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_:b441723695 , _:b441723688 , _:b441723689 , _:b441723690 , _:b441723691 , _:b441723684 , _:b441723685 , _:b441723686 , _:b441723687 , _:b441723680 , _:b441723681 , _:b441723682 , _:b441723683 , _:b441723708 , _:b441723709 , _:b441723710 , _:b441723711 , _:b441723704 , _:b441723705 , _:b441723706 , _:b441723707 , _:b441723700 , _:b441723701 , _:b441723702 , _:b441723703 , _:b441723696 , _:b441723697 , _:b441723698 , _:b441723699 , _:b441723660 , _:b441723661 , _:b441723662 , _:b441723663 , _:b441723656 , _:b441723657 , _:b441723658 , _:b441723659 , _:b441723652 , _:b441723653 , _:b441723654 , _:b441723655 , _:b441723648 , _:b441723649 , _:b441723650 , _:b441723651 , _:b441723676 , _:b441723677 , _:b441723678 , _:b441723679 , _:b441723672 , _:b441723673 , _:b441723674 , _:b441723675 , _:b441723668 , _:b441723669 , _:b441723670 , _:b441723671 , _:b441723664 , _:b441723665 , _:b441723666 , _:b441723667 , _:b441723756 , _:b441723757 , _:b441723758 , _:b441723759 , _:b441723752 , 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_:b441723819 , _:b441723812 , _:b441723813 , _:b441723814 , _:b441723815 , _:b441723808 , _:b441723809 , _:b441723810 , _:b441723811 , _:b441723836 , _:b441723837 , _:b441723838 , _:b441723839 , _:b441723832 , _:b441723833 , _:b441723834 , _:b441723835 , _:b441723828 , _:b441723829 , _:b441723830 , _:b441723831 , _:b441723824 , _:b441723825 , _:b441723826 , _:b441723827 , _:b441723788 , _:b441723789 , _:b441723790 , _:b441723791 , _:b441723784 , _:b441723785 , _:b441723786 , _:b441723787 , _:b441723780 , _:b441723781 , _:b441723782 , _:b441723783 , _:b441723776 , _:b441723777 , _:b441723778 , _:b441723779 , _:b441723804 , _:b441723805 , _:b441723806 , _:b441723807 , _:b441723800 , _:b441723801 , _:b441723802 , _:b441723803 , _:b441723796 , _:b441723797 , _:b441723798 , _:b441723799 , _:b441723792 , _:b441723793 , _:b441723794 , _:b441723795 , _:b441723884 , _:b441723885 , _:b441723886 , _:b441723887 , _:b441723880 , _:b441723881 , _:b441723882 , _:b441723883 , _:b441723876 , _:b441723877 , _:b441723878 , _:b441723879 , _:b441723872 , _:b441723873 , _:b441723874 , _:b441723875 , _:b441723900 , _:b441723901 , _:b441723902 , _:b441723903 , _:b441723896 , _:b441723897 , _:b441723898 , _:b441723899 , _:b441723892 , _:b441723893 , _:b441723894 , _:b441723895 , _:b441723888 , _:b441723889 , _:b441723890 , _:b441723891 , _:b441723852 , _:b441723853 , _:b441723854 , _:b441723855 , _:b441723848 , _:b441723849 , _:b441723850 , _:b441723851 , _:b441723844 , _:b441723845 , _:b441723846 , _:b441723847 , _:b441723840 , _:b441723841 , _:b441723842 , _:b441723843 , _:b441723868 , _:b441723869 , _:b441723870 , _:b441723871 , _:b441723864 , _:b441723865 , _:b441723866 , _:b441723867 , _:b441723860 , _:b441723861 , _:b441723862 , _:b441723863 , _:b441723856 , _:b441723857 , _:b441723858 , _:b441723859 ; ns1:pmcid "PMC0" ; bibo:doi "10.1002%2Fcm.20472" . @prefix ns4: . ns4:contains _:b8584676 . _:b8584676 rdf:type ns4:Section . @prefix dc: . _:b8584676 dc:title "introduction" ; ns4:contains _:b8584692 , _:b8584693 , _:b8584694 , _:b8584695 , _:b8584688 , _:b8584689 , _:b8584690 , _:b8584691 , _:b8584700 , _:b8584701 , _:b8584702 , _:b8584703 , _:b8584696 , _:b8584697 , _:b8584698 , _:b8584699 , _:b8584677 , _:b8584678 , _:b8584679 , _:b8584684 , _:b8584685 , _:b8584686 , _:b8584687 , _:b8584680 , _:b8584681 , _:b8584682 , _:b8584683 , _:b8584820 , _:b8584821 , _:b8584822 , _:b8584823 , _:b8584816 , _:b8584817 , _:b8584818 , _:b8584819 , _:b8584804 , _:b8584805 , _:b8584806 , _:b8584807 , _:b8584800 , _:b8584801 , _:b8584802 , _:b8584803 , _:b8584812 , _:b8584813 , _:b8584814 , _:b8584815 , _:b8584808 , _:b8584809 , _:b8584810 , _:b8584811 , _:b8584788 , _:b8584789 , _:b8584790 , _:b8584791 , _:b8584784 , _:b8584785 , _:b8584786 , _:b8584787 , _:b8584796 , _:b8584797 , _:b8584798 , _:b8584799 , _:b8584792 , _:b8584793 , _:b8584794 , _:b8584795 , _:b8584772 , _:b8584773 , _:b8584774 , _:b8584775 , _:b8584768 , _:b8584769 , _:b8584770 , _:b8584771 , _:b8584780 , _:b8584781 , _:b8584782 , _:b8584783 , _:b8584776 , _:b8584777 , _:b8584778 , _:b8584779 , _:b8584756 , _:b8584757 , _:b8584758 , _:b8584759 , _:b8584752 , _:b8584753 , _:b8584754 , _:b8584755 , _:b8584764 , _:b8584765 , _:b8584766 , _:b8584767 , _:b8584760 , _:b8584761 , _:b8584762 , _:b8584763 , _:b8584740 , _:b8584741 , _:b8584742 , _:b8584743 , _:b8584736 , _:b8584737 , _:b8584738 , _:b8584739 , _:b8584748 , _:b8584749 , _:b8584750 , _:b8584751 , _:b8584744 , _:b8584745 , _:b8584746 , _:b8584747 , _:b8584724 , _:b8584725 , _:b8584726 , _:b8584727 , _:b8584720 , _:b8584721 , _:b8584722 , _:b8584723 , _:b8584732 , _:b8584733 , _:b8584734 , _:b8584735 , _:b8584728 , _:b8584729 , _:b8584730 , _:b8584731 , _:b8584708 , _:b8584709 , _:b8584710 , _:b8584711 , _:b8584704 , _:b8584705 , _:b8584706 , _:b8584707 , _:b8584716 , _:b8584717 , _:b8584718 , _:b8584719 , _:b8584712 , _:b8584713 , _:b8584714 , _:b8584715 . _:b8584677 rdf:type ns1:Context ; rdf:value "Rho-kinase, originally identified as an effector of the small GTPase Rho [Leung et al., >>1995<<; Ishizaki et al., 1996; Matsui et al., 1996], plays a major role in mediating rearrangements of the actomyosin cytoskeleton downstream of Rho." ; ns1:mentions . _:b8584678 rdf:type ns1:Context ; rdf:value "Rho-kinase, originally identified as an effector of the small GTPase Rho [Leung et al., 1995; Ishizaki et al., >>1996<<; Matsui et al., 1996], plays a major role in mediating rearrangements of the actomyosin cytoskeleton downstream of Rho." ; ns1:mentions . _:b8584679 rdf:type ns1:Context ; rdf:value "Rho-kinase, originally identified as an effector of the small GTPase Rho [Leung et al., 1995; Ishizaki et al., 1996; Matsui et al., >>1996<<], plays a major role in mediating rearrangements of the actomyosin cytoskeleton downstream of Rho." ; ns1:mentions . _:b8584680 rdf:type ns1:Context ; rdf:value "Rho family small GTPases, such as Rho, Rac, and Cdc42, regulate cytoskeletal reorganization in different ways [Kaibuchi et al., >>1999<<; Jaffe and Hall, 2005]." ; ns1:mentions . _:b8584681 rdf:type ns1:Context ; rdf:value "Rho family small GTPases, such as Rho, Rac, and Cdc42, regulate cytoskeletal reorganization in different ways [Kaibuchi et al., 1999; Jaffe and Hall, >>2005<<]. The functions of these GTPases have been primarily investigated with regard to their effects of actin filaments. Rho regulates stress fiber formation and cell contraction, whereas Rac and Cdc42 regulate the formation of lamellipodia and" ; ns1:mentions . _:b8584682 rdf:type ns1:Context ; rdf:value "Rho regulates stress fiber formation and cell contraction, whereas Rac and Cdc42 regulate the formation of lamellipodia and filopodia, respectively, and promote protrusive activities [Hall, >>2005<<]. Rho family GTPases also modulate microtubule dynamics and cell polarity. Furthermore, in addition to Rho-kinase, many other Rho effectors with various functions have been identified, including the myosin phosphatase-targeting subunit 1" ; ns1:mentions . _:b8584683 rdf:type ns1:Context ; rdf:value "For example, Rho-kinase functions together with MYPT1 and mDia to achieve stress fiber and focal adhesion formation downstream of Rho [Amano et al., >>2000<<; Narumiya et al., 2009]." ; ns1:mentions . _:b8584684 rdf:type ns1:Context ; rdf:value "For example, Rho-kinase functions together with MYPT1 and mDia to achieve stress fiber and focal adhesion formation downstream of Rho [Amano et al., 2000; Narumiya et al., >>2009<<]. In this review, we will focus on the structure, function, and modes of action of Rho-kinase." ; ns1:mentions . _:b8584685 rdf:type ns1:Context ; rdf:value "Rho-kinase has N- and C-terminal extension segments outside the catalytic domain that form an intermolecular head-to-head homodimer, keeping it in an active conformation [Yamaguchi et al., 2006a; Jacobs et al., 2006] (Fig." ; ns1:mentions . _:b8584686 rdf:type ns1:Context ; rdf:value "Rho-kinase has N- and C-terminal extension segments outside the catalytic domain that form an intermolecular head-to-head homodimer, keeping it in an active conformation [Yamaguchi et al., 2006a; Jacobs et al., >>2006<<] (Fig. 2). Interestingly, phosphorylation at the activation loop or C-terminal hydrophobic motif, which is necessary for most of other AGC kinases such as PKC and Akt, is absent from the Rho-kinase catalytic domain in its dimerized active" ; ns1:mentions . _:b8584687 rdf:type ns1:Context ; rdf:value "at the activation loop or C-terminal hydrophobic motif, which is necessary for most of other AGC kinases such as PKC and Akt, is absent from the Rho-kinase catalytic domain in its dimerized active conformation [Yamaguchi et al., 2006a]. The Rho-binding region of Rho-kinase also forms a parallel coiled-coil structure [Shimizu et al., 2003; Dvorsky et al., 2004], supporting the idea that Rho-kinase dimerizes in a parallel manner." ; ns1:mentions . _:b8584688 rdf:type ns1:Context ; rdf:value "The Rho-binding region of Rho-kinase also forms a parallel coiled-coil structure [Shimizu et al., >>2003<<; Dvorsky et al., 2004], supporting the idea that Rho-kinase dimerizes in a parallel manner." ; ns1:mentions . _:b8584689 rdf:type ns1:Context ; rdf:value "The Rho-binding region of Rho-kinase also forms a parallel coiled-coil structure [Shimizu et al., 2003; Dvorsky et al., >>2004<<], supporting the idea that Rho-kinase dimerizes in a parallel manner." ; ns1:mentions . _:b8584690 rdf:type ns1:Context ; rdf:value "Consistent with this, Rho-kinase is found as a multimer in the cell [Chen et al., >>2002<<]." ; ns1:mentions . _:b8584691 rdf:type ns1:Context ; rdf:value "interaction between active Rho (Rho\u00B7GTP) and the Rho-binding domain releases this inhibition is based on several lines of evidence: (1) deletion of the C-terminal portion results in constitutive activation of Rho-kinase [Leung et al., >>1996<<; Amano et al., 1997; Ishizaki et al., 1997], (2) the C-terminal segment interacts with and inhibits the constitutively active catalytic fragment both in vitro and in vivo [Amano et al., 1999], and (3) an antibody against the Rho-binding" ; ns1:mentions . _:b8584692 rdf:type ns1:Context ; rdf:value "active Rho (Rho\u00B7GTP) and the Rho-binding domain releases this inhibition is based on several lines of evidence: (1) deletion of the C-terminal portion results in constitutive activation of Rho-kinase [Leung et al., 1996; Amano et al., >>1997<<; Ishizaki et al., 1997], (2) the C-terminal segment interacts with and inhibits the constitutively active catalytic fragment both in vitro and in vivo [Amano et al., 1999], and (3) an antibody against the Rho-binding domain of Rho-kinase" ; ns1:mentions . _:b8584693 rdf:type ns1:Context ; rdf:value "the Rho-binding domain releases this inhibition is based on several lines of evidence: (1) deletion of the C-terminal portion results in constitutive activation of Rho-kinase [Leung et al., 1996; Amano et al., 1997; Ishizaki et al., >>1997<<], (2) the C-terminal segment interacts with and inhibits the constitutively active catalytic fragment both in vitro and in vivo [Amano et al., 1999], and (3) an antibody against the Rho-binding domain of Rho-kinase enhances its kinase" ; ns1:mentions . _:b8584694 rdf:type ns1:Context ; rdf:value "activation of Rho-kinase [Leung et al., 1996; Amano et al., 1997; Ishizaki et al., 1997], (2) the C-terminal segment interacts with and inhibits the constitutively active catalytic fragment both in vitro and in vivo [Amano et al., >>1999<<], and (3) an antibody against the Rho-binding domain of Rho-kinase enhances its kinase activity in vitro (unpublished observation)." ; ns1:mentions . _:b8584695 rdf:type ns1:Context ; rdf:value "In addition to Rho, certain lipids such as arachidonic acid can activate Rho-kinase via its PH domain [Araki et al., >>2001<<]. Proteolytic cleavage at the C-terminus by caspase-3 and granzyme B is also reported to activate ROCK1 and ROCK2, leading to plasma membrane blebbing during apoptosis [Coleman et al., 2001; Sebbagh et al., 2001; Sebbagh et al., 2005]." ; ns1:mentions . _:b8584696 rdf:type ns1:Context ; rdf:value "Proteolytic cleavage at the C-terminus by caspase-3 and granzyme B is also reported to activate ROCK1 and ROCK2, leading to plasma membrane blebbing during apoptosis [Coleman et al., >>2001<<; Sebbagh et al., 2001; Sebbagh et al., 2005]." ; ns1:mentions . _:b8584697 rdf:type ns1:Context ; rdf:value "Proteolytic cleavage at the C-terminus by caspase-3 and granzyme B is also reported to activate ROCK1 and ROCK2, leading to plasma membrane blebbing during apoptosis [Coleman et al., 2001; Sebbagh et al., >>2001<<; Sebbagh et al., 2005]." ; ns1:mentions . _:b8584698 rdf:type ns1:Context ; rdf:value "Proteolytic cleavage at the C-terminus by caspase-3 and granzyme B is also reported to activate ROCK1 and ROCK2, leading to plasma membrane blebbing during apoptosis [Coleman et al., 2001; Sebbagh et al., 2001; Sebbagh et al., >>2005<<]. Other small GTPases besides Rho - Rnd3/RhoE, Gem and Rad - can bind Rho-kinase outside of the Rho-binding region and inhibit its function [Ward et al., 2002; Riento et al., 2003; Komander et al., 2008]. It has also been reported that" ; ns1:mentions . _:b8584699 rdf:type ns1:Context ; rdf:value "Other small GTPases besides Rho - Rnd3/RhoE, Gem and Rad - can bind Rho-kinase outside of the Rho-binding region and inhibit its function [Ward et al., >>2002<<; Riento et al., 2003; Komander et al., 2008]." ; ns1:mentions . _:b8584700 rdf:type ns1:Context ; rdf:value "Other small GTPases besides Rho - Rnd3/RhoE, Gem and Rad - can bind Rho-kinase outside of the Rho-binding region and inhibit its function [Ward et al., 2002; Riento et al., >>2003<<; Komander et al., 2008]." ; ns1:mentions . _:b8584701 rdf:type ns1:Context ; rdf:value "Other small GTPases besides Rho - Rnd3/RhoE, Gem and Rad - can bind Rho-kinase outside of the Rho-binding region and inhibit its function [Ward et al., 2002; Riento et al., 2003; Komander et al., >>2008<<]. It has also been reported that PDK1 directly binds to ROCK1 in competition with RhoE, leading to the release of ROCK1 from RhoE and activation [Pinner and Sahai, 2008]." ; ns1:mentions . _:b8584702 rdf:type ns1:Context ; rdf:value "It has also been reported that PDK1 directly binds to ROCK1 in competition with RhoE, leading to the release of ROCK1 from RhoE and activation [Pinner and Sahai, >>2008<<]." ; ns1:mentions . _:b8584703 rdf:type ns1:Context ; rdf:value "proteins are ubiquitously expressed in most tissues; however, higher levels of ROCK2 are found in brain and muscles whereas higher levels of ROCK1 are found in non-neuronal tissues including liver, lung and testis [Leung et al., >>1996<<; Nakagawa et al., 1996]. So far, several functional differences between ROCK1 and ROCK2 have been reported." ; ns1:mentions . _:b8584704 rdf:type ns1:Context ; rdf:value "expressed in most tissues; however, higher levels of ROCK2 are found in brain and muscles whereas higher levels of ROCK1 are found in non-neuronal tissues including liver, lung and testis [Leung et al., 1996; Nakagawa et al., >>1996<<]. So far, several functional differences between ROCK1 and ROCK2 have been reported." ; ns1:mentions . _:b8584705 rdf:type ns1:Context ; rdf:value "ROCK1 is specifically cleaved by caspase-3, whereas ROCK2 is cleaved by granzyme B [Coleman et al., >>2001<<; Sebbagh et al., 2001; Sebbagh et al., 2005]." ; ns1:mentions . _:b8584706 rdf:type ns1:Context ; rdf:value "ROCK1 is specifically cleaved by caspase-3, whereas ROCK2 is cleaved by granzyme B [Coleman et al., 2001; Sebbagh et al., >>2001<<; Sebbagh et al., 2005]." ; ns1:mentions . _:b8584707 rdf:type ns1:Context ; rdf:value "ROCK1 is specifically cleaved by caspase-3, whereas ROCK2 is cleaved by granzyme B [Coleman et al., 2001; Sebbagh et al., 2001; Sebbagh et al., >>2005<<]. RhoE preferentially binds ROCK1, but not ROCK2, whereas MYPT1 binds only ROCK2 [Komander et al., 2008; Wang et al, 2009]. Gene silencing experiments also suggest different cellular functions for these two proteins, ROCK1 appears to be" ; ns1:mentions . _:b8584708 rdf:type ns1:Context ; rdf:value "RhoE preferentially binds ROCK1, but not ROCK2, whereas MYPT1 binds only ROCK2 [Komander et al., >>2008<<; Wang et al, 2009]." ; ns1:mentions . _:b8584709 rdf:type ns1:Context ; rdf:value "RhoE preferentially binds ROCK1, but not ROCK2, whereas MYPT1 binds only ROCK2 [Komander et al., 2008; Wang et al, >>2009<<]. Gene silencing experiments also suggest different cellular functions for these two proteins, ROCK1 appears to be essential for the formation of stress fibers, whereas ROCK2 appears to be necessary for phagocytosis and cell contraction," ; ns1:mentions . _:b8584710 rdf:type ns1:Context ; rdf:value "for these two proteins, ROCK1 appears to be essential for the formation of stress fibers, whereas ROCK2 appears to be necessary for phagocytosis and cell contraction, both of which are dependent on MLC phosphorylation [Yoneda et al., >>2005<<; Wang et al., 2009]." ; ns1:mentions . _:b8584711 rdf:type ns1:Context ; rdf:value "ROCK1 appears to be essential for the formation of stress fibers, whereas ROCK2 appears to be necessary for phagocytosis and cell contraction, both of which are dependent on MLC phosphorylation [Yoneda et al., 2005; Wang et al., >>2009<<]. Most if not all mice carrying a homozygous deletion of the either the ROCK2 or ROCK1 allele show embryonic or postnatal lethality, respectively, whereas heterozygous mice are fertile and appear normal [Thumkeo et al., 2003; Shimizu et" ; ns1:mentions . _:b8584712 rdf:type ns1:Context ; rdf:value "Most if not all mice carrying a homozygous deletion of the either the ROCK2 or ROCK1 allele show embryonic or postnatal lethality, respectively, whereas heterozygous mice are fertile and appear normal [Thumkeo et al., >>2003<<; Shimizu et al., 2005; Thumkeo et al., 2005]." ; ns1:mentions . _:b8584713 rdf:type ns1:Context ; rdf:value "if not all mice carrying a homozygous deletion of the either the ROCK2 or ROCK1 allele show embryonic or postnatal lethality, respectively, whereas heterozygous mice are fertile and appear normal [Thumkeo et al., 2003; Shimizu et al., >>2005<<; Thumkeo et al., 2005]. However, the question of whether these two Rho-kinase proteins are qualitatively different or expressed at different abundances in tissues remains unanswered." ; ns1:mentions . _:b8584714 rdf:type ns1:Context ; rdf:value "a homozygous deletion of the either the ROCK2 or ROCK1 allele show embryonic or postnatal lethality, respectively, whereas heterozygous mice are fertile and appear normal [Thumkeo et al., 2003; Shimizu et al., 2005; Thumkeo et al., >>2005<<]. However, the question of whether these two Rho-kinase proteins are qualitatively different or expressed at different abundances in tissues remains unanswered." ; ns1:mentions . _:b8584715 rdf:type ns1:Context ; rdf:value "To elucidate the physiological roles of Rho-kinase, small molecule inhibitors have been developed and investigated in various cell types and animal models [Mueller et al., 2005; Shimokawa and Rashid, >>2007<<]. Fasudil (HA-1077) and Y-27632 have been broadly used as Rho-kinase selective inhibitors and function in an ATP-competitive manner." ; ns1:mentions . _:b8584716 rdf:type ns1:Context ; rdf:value "Y-27632 was identified by its ability to inhibit phenylephrine-induced contraction of a rabbit aortic strip and contains a 4-aminopyridine ring [Uehata et al., >>1997<<]. Structural analyses of the Rho-kinase (ROCK2)-Fasudil complex [Yamaguchi et al., 2006a], Rho-kinase (ROCK2)-Y-27632 complex [Yamaguchi et al., 2006b], and ROCK1-Y-27632 complex [Jacobs et al., 2006] revealed the inhibitors cause an" ; ns1:mentions . _:b8584717 rdf:type ns1:Context ; rdf:value "Structural analyses of the Rho-kinase (ROCK2)-Fasudil complex [Yamaguchi et al., 2006a], Rho-kinase (ROCK2)-Y-27632 complex [Yamaguchi et al., 2006b], and ROCK1-Y-27632 complex [Jacobs et al., 2006] revealed the inhibitors cause an induced-fit conformational change to increase contacts with Rho-kinase phosphate loop, which" ; ns1:mentions . _:b8584718 rdf:type ns1:Context ; rdf:value "Structural analyses of the Rho-kinase (ROCK2)-Fasudil complex [Yamaguchi et al., 2006a], Rho-kinase (ROCK2)-Y-27632 complex [Yamaguchi et al., 2006b], and ROCK1-Y-27632 complex [Jacobs et al., 2006] revealed the inhibitors cause an induced-fit conformational change to increase contacts with Rho-kinase phosphate loop, which may account for their specificity." ; ns1:mentions . _:b8584719 rdf:type ns1:Context ; rdf:value "Structural analyses of the Rho-kinase (ROCK2)-Fasudil complex [Yamaguchi et al., 2006a], Rho-kinase (ROCK2)-Y-27632 complex [Yamaguchi et al., 2006b], and ROCK1-Y-27632 complex [Jacobs et al., >>2006<<] revealed the inhibitors cause an induced-fit conformational change to increase contacts with Rho-kinase phosphate loop, which may account for their specificity." ; ns1:mentions . _:b8584720 rdf:type ns1:Context ; rdf:value "Several pharmaceutical companies are investing in the development of Rho-kinase inhibitors for the treatment of certain diseases, such as glaucoma (see [Hahmann and Schroeter, >>2010<<] for a review)." ; ns1:mentions . _:b8584721 rdf:type ns1:Context ; rdf:value "SubstrateEffect of phosphorylationCellular functionReferenceMicrofilament\u2003MYPT1Inhibition of MLC phosphataseIncrease in cell contraction[Kimura et al., 1996]\u2003MLCActivation of myosin ATPaseIncrease in cell contraction[Amano et al., >>1996<<]\u2003ERMMaintenance of crosslinkingMicrovilli formation?" ; ns1:mentions . _:b8584722 rdf:type ns1:Context ; rdf:value "[Fukata et al., >>1998<<] [Oshiro et al., 1998] [Matsui et al., 1998]\u2003AdducinEnhancement of F-actin bindingCell migration[Fukata et al., 1999]\u2003LIMK1/2Activation of cofilin phosphorylationStress fiber formation[Maekawa et al., 1999] [Ohashi et al., 2000]" ; ns1:mentions . _:b8584723 rdf:type ns1:Context ; rdf:value "[Fukata et al., 1998] [Oshiro et al., >>1998<<] [Matsui et al., 1998]\u2003AdducinEnhancement of F-actin bindingCell migration[Fukata et al., 1999]\u2003LIMK1/2Activation of cofilin phosphorylationStress fiber formation[Maekawa et al., 1999] [Ohashi et al., 2000]\u2003CalponinInhibition of F-actin" ; ns1:mentions . _:b8584724 rdf:type ns1:Context ; rdf:value "[Fukata et al., 1998] [Oshiro et al., 1998] [Matsui et al., >>1998<<]\u2003AdducinEnhancement of F-actin bindingCell migration[Fukata et al., 1999]\u2003LIMK1/2Activation of cofilin phosphorylationStress fiber formation[Maekawa et al., 1999] [Ohashi et al., 2000]\u2003CalponinInhibition of F-actin bindingn." ; ns1:mentions . _:b8584725 rdf:type ns1:Context ; rdf:value "[Fukata et al., 1998] [Oshiro et al., 1998] [Matsui et al., 1998]\u2003AdducinEnhancement of F-actin bindingCell migration[Fukata et al., >>1999<<]\u2003LIMK1/2Activation of cofilin phosphorylationStress fiber formation[Maekawa et al., 1999] [Ohashi et al., 2000]\u2003CalponinInhibition of F-actin bindingn." ; ns1:mentions . _:b8584726 rdf:type ns1:Context ; rdf:value "[Fukata et al., 1998] [Oshiro et al., 1998] [Matsui et al., 1998]\u2003AdducinEnhancement of F-actin bindingCell migration[Fukata et al., 1999]\u2003LIMK1/2Activation of cofilin phosphorylationStress fiber formation[Maekawa et al., >>1999<<] [Ohashi et al., 2000]\u2003CalponinInhibition of F-actin bindingn." ; ns1:mentions . _:b8584727 rdf:type ns1:Context ; rdf:value "al., 1998] [Oshiro et al., 1998] [Matsui et al., 1998]\u2003AdducinEnhancement of F-actin bindingCell migration[Fukata et al., 1999]\u2003LIMK1/2Activation of cofilin phosphorylationStress fiber formation[Maekawa et al., 1999] [Ohashi et al., >>2000<<]\u2003CalponinInhibition of F-actin bindingn.d.[Kaneko et al., 2000]\u2003CPI-17Inhibition of MLC phosphataseIncrease in cell contraction[Koyama et al., 2000]\u2003NHE1n." ; ns1:mentions . _:b8584728 rdf:type ns1:Context ; rdf:value "[Kaneko et al., >>2000<<]\u2003CPI-17Inhibition of MLC phosphataseIncrease in cell contraction[Koyama et al., 2000]\u2003NHE1n." ; ns1:mentions . _:b8584729 rdf:type ns1:Context ; rdf:value "[Kaneko et al., 2000]\u2003CPI-17Inhibition of MLC phosphataseIncrease in cell contraction[Koyama et al., >>2000<<]\u2003NHE1n.d.Stress fiber formation[Tominaga and Barber, 1998] [Denker et al., 2000]\u2003MARCKSInhibition of F-actin bindingn.d.[Nagumo et al., 2001]\u2003EF1\u03B1Inhibition of F-actin bindingn.d.[Izawa et al., 2000]\u2003Troponin I/Tn.d.Inhibition of Ca2+" ; ns1:mentions . _:b8584730 rdf:type ns1:Context ; rdf:value "Stress fiber formation[Tominaga and Barber, >>1998<<] [Denker et al., 2000]\u2003MARCKSInhibition of F-actin bindingn." ; ns1:mentions . _:b8584731 rdf:type ns1:Context ; rdf:value "Stress fiber formation[Tominaga and Barber, 1998] [Denker et al., >>2000<<]\u2003MARCKSInhibition of F-actin bindingn." ; ns1:mentions . _:b8584732 rdf:type ns1:Context ; rdf:value "d.[Nagumo et al., >>2001<<]\u2003EF1\u03B1Inhibition of F-actin bindingn.d.[Izawa et al., 2000]\u2003Troponin I/Tn." ; ns1:mentions . _:b8584733 rdf:type ns1:Context ; rdf:value "[Nagumo et al., 2001]\u2003EF1\u03B1Inhibition of F-actin bindingn.d.[Izawa et al., >>2000<<]\u2003Troponin I/Tn.d." ; ns1:mentions . _:b8584734 rdf:type ns1:Context ; rdf:value "Inhibition of Ca2+ response in cardiac muscle[Vahebi et al., >>2005<<]\u2003ProfilinInhibition of G-actin bindingDecrease in polyQ aggregation[Shao et al., 2008] [Bauer et al., 2009]Microtubule\u2003MAP2/TauInhibition of tubulin polymerizationInhibition of neurite elongation?" ; ns1:mentions . _:b8584735 rdf:type ns1:Context ; rdf:value "Inhibition of Ca2+ response in cardiac muscle[Vahebi et al., 2005]\u2003ProfilinInhibition of G-actin bindingDecrease in polyQ aggregation[Shao et al., >>2008<<] [Bauer et al., 2009]Microtubule\u2003MAP2/TauInhibition of tubulin polymerizationInhibition of neurite elongation?" ; ns1:mentions . _:b8584736 rdf:type ns1:Context ; rdf:value "Inhibition of Ca2+ response in cardiac muscle[Vahebi et al., 2005]\u2003ProfilinInhibition of G-actin bindingDecrease in polyQ aggregation[Shao et al., 2008] [Bauer et al., >>2009<<]Microtubule\u2003MAP2/TauInhibition of tubulin polymerizationInhibition of neurite elongation?" ; ns1:mentions . _:b8584737 rdf:type ns1:Context ; rdf:value "[Amano et al., >>2003<<]\u2003CRMP2Inhibition of tubulin polymerizationGrowth cone collapse[Arimura et al., 2000; Arimura et al., 2005]\u2003DoublecortinInhibition of microtubule bundlingNeuronal migration?" ; ns1:mentions . _:b8584738 rdf:type ns1:Context ; rdf:value "[Amano et al., 2003]\u2003CRMP2Inhibition of tubulin polymerizationGrowth cone collapse[Arimura et al., >>2000<<; Arimura et al., 2005]\u2003DoublecortinInhibition of microtubule bundlingNeuronal migration?" ; ns1:mentions . _:b8584739 rdf:type ns1:Context ; rdf:value "[Amano et al., 2003]\u2003CRMP2Inhibition of tubulin polymerizationGrowth cone collapse[Arimura et al., 2000; Arimura et al., >>2005<<]\u2003DoublecortinInhibition of microtubule bundlingNeuronal migration?" ; ns1:mentions . _:b8584740 rdf:type ns1:Context ; rdf:value "[Amano et al., 2003]\u2003CRMP2Inhibition of tubulin polymerizationGrowth cone collapse[Arimura et al., 2000; Arimura et al., 2005]\u2003DoublecortinInhibition of microtubule bundlingNeuronal migration?[Amano et al., >>2010<<]Intermediate filament\u2003GFAPDepolymerizationProgression of cytokinesis[Yasui et al., 1998]\u2003VimentinDepolymerizationProgression of cytokinesis[Goto et al., 1998]\u2003Neurofilament (NF-L)DepolymerizationNeurite retraction[Hashimoto et al.," ; ns1:mentions . _:b8584741 rdf:type ns1:Context ; rdf:value "[Amano et al., 2010]Intermediate filament\u2003GFAPDepolymerizationProgression of cytokinesis[Yasui et al., >>1998<<]\u2003VimentinDepolymerizationProgression of cytokinesis[Goto et al., 1998]\u2003Neurofilament (NF-L)DepolymerizationNeurite retraction[Hashimoto et al., 1998]Signaling crosstalk\u2003Par3Dissociation of Par3/Tiam1 from Par6/aPKCControl of cell" ; ns1:mentions . _:b8584742 rdf:type ns1:Context ; rdf:value "[Amano et al., 2010]Intermediate filament\u2003GFAPDepolymerizationProgression of cytokinesis[Yasui et al., 1998]\u2003VimentinDepolymerizationProgression of cytokinesis[Goto et al., >>1998<<]\u2003Neurofilament (NF-L)DepolymerizationNeurite retraction[Hashimoto et al., 1998]Signaling crosstalk\u2003Par3Dissociation of Par3/Tiam1 from Par6/aPKCControl of cell migration[Nakayama et al., 2008]\u2003STEFInhibition of GEF activity?" ; ns1:mentions . _:b8584743 rdf:type ns1:Context ; rdf:value "filament\u2003GFAPDepolymerizationProgression of cytokinesis[Yasui et al., 1998]\u2003VimentinDepolymerizationProgression of cytokinesis[Goto et al., 1998]\u2003Neurofilament (NF-L)DepolymerizationNeurite retraction[Hashimoto et al., >>1998<<]Signaling crosstalk\u2003Par3Dissociation of Par3/Tiam1 from Par6/aPKCControl of cell migration[Nakayama et al., 2008]\u2003STEFInhibition of GEF activity?" ; ns1:mentions . _:b8584744 rdf:type ns1:Context ; rdf:value "of cytokinesis[Goto et al., 1998]\u2003Neurofilament (NF-L)DepolymerizationNeurite retraction[Hashimoto et al., 1998]Signaling crosstalk\u2003Par3Dissociation of Par3/Tiam1 from Par6/aPKCControl of cell migration[Nakayama et al., >>2008<<]\u2003STEFInhibition of GEF activity?Inhibition of neurite outgrowth?[Takefuji et al., 2007]\u2003p190RhoGAPInhibition of Rnd bindingPositive feedback signal of Rho?" ; ns1:mentions . _:b8584745 rdf:type ns1:Context ; rdf:value "[Takefuji et al., >>2007<<]\u2003p190RhoGAPInhibition of Rnd bindingPositive feedback signal of Rho?" ; ns1:mentions . _:b8584746 rdf:type ns1:Context ; rdf:value "[Mori et al., >>2009<<]\u2003eNOSInactivation of eNOSCell contraction?[Sugimoto et al., 2007]\u2003PTENActivation of phosphatase activity?" ; ns1:mentions . _:b8584747 rdf:type ns1:Context ; rdf:value "[Li et al., >>2005<<]\u2003FilGAPActivation of RacGAP activityLamella formation, cell polarity[Ohta et al., 2006]\u2003IRS1Positive/negative regulation of insulin signal?" ; ns1:mentions . _:b8584748 rdf:type ns1:Context ; rdf:value "[Li et al., 2005]\u2003FilGAPActivation of RacGAP activityLamella formation, cell polarity[Ohta et al., >>2006<<]\u2003IRS1Positive/negative regulation of insulin signal?" ; ns1:mentions . _:b8584749 rdf:type ns1:Context ; rdf:value "[Li et al., 2005]\u2003FilGAPActivation of RacGAP activityLamella formation, cell polarity[Ohta et al., 2006]\u2003IRS1Positive/negative regulation of insulin signal?[Furukawa et al., >>2005<<]\u2003EndophilinInhibition of CIN85 bindingInhibition of EGFR endocytosis[Kaneko et al., 2005]\u2003P300Increase in acetyltransferase activityEnhancement of transcription[Tanaka et al., 2006]\u2003RhoEStabilizationDecrease of stress fibers[Komander et" ; ns1:mentions . _:b8584750 rdf:type ns1:Context ; rdf:value "[Furukawa et al., 2005]\u2003EndophilinInhibition of CIN85 bindingInhibition of EGFR endocytosis[Kaneko et al., >>2005<<]\u2003P300Increase in acetyltransferase activityEnhancement of transcription[Tanaka et al., 2006]\u2003RhoEStabilizationDecrease of stress fibers[Komander et al., 2008; Riento et al.," ; ns1:mentions . _:b8584751 rdf:type ns1:Context ; rdf:value "[Furukawa et al., 2005]\u2003EndophilinInhibition of CIN85 bindingInhibition of EGFR endocytosis[Kaneko et al., 2005]\u2003P300Increase in acetyltransferase activityEnhancement of transcription[Tanaka et al., >>2006<<]\u2003RhoEStabilizationDecrease of stress fibers[Komander et al., 2008; Riento et al.," ; ns1:mentions . _:b8584752 rdf:type ns1:Context ; rdf:value "of CIN85 bindingInhibition of EGFR endocytosis[Kaneko et al., 2005]\u2003P300Increase in acetyltransferase activityEnhancement of transcription[Tanaka et al., 2006]\u2003RhoEStabilizationDecrease of stress fibers[Komander et al., >>2008<<; Riento et al.," ; ns1:mentions . _:b8584753 rdf:type ns1:Context ; rdf:value "bindingInhibition of EGFR endocytosis[Kaneko et al., 2005]\u2003P300Increase in acetyltransferase activityEnhancement of transcription[Tanaka et al., 2006]\u2003RhoEStabilizationDecrease of stress fibers[Komander et al., 2008; Riento et al., >>2003<<" ; ns1:mentions . _:b8584754 rdf:type ns1:Context ; rdf:value "MLC phosphatase is composed of the catalytic subunit (PP1c\u03B4) and two regulatory subunits, myosin phosphatase-targeting subunit 1 (MYPT1) and M20 [Ito et al., >>2004<<]. Rho-kinase phosphorylates MYPT1 at two inhibitory sites, Thr853 and Thr696, resulting in a decrease in MLC phosphatase activity and an increase in phosphorylated MLC [Kimura et al., 1996]. Rho-kinase can also phosphorylate MLC at Ser19" ; ns1:mentions . _:b8584755 rdf:type ns1:Context ; rdf:value "Rho-kinase can also phosphorylate MLC at Ser19 to increases myosin ATPase activity at least in vitro [Amano et al., >>1996<<], although a direct contribution of Rho-kinase to phospho-MLC levels in vivo is not yet proved." ; ns1:mentions . _:b8584756 rdf:type ns1:Context ; rdf:value "CPI-17 has an inhibitory effect on MLC phosphatase when it is phosphorylated by PKC at Thr38 and is also reported to be phosphorylated by Rho-kinase at the same site [Kitazawa et al., >>2000<<] [Koyama et al., 2000]." ; ns1:mentions . _:b8584757 rdf:type ns1:Context ; rdf:value "CPI-17 has an inhibitory effect on MLC phosphatase when it is phosphorylated by PKC at Thr38 and is also reported to be phosphorylated by Rho-kinase at the same site [Kitazawa et al., 2000] [Koyama et al., >>2000<<]. Several studies using permeabilized smooth muscle and selective inhibitors have shown that Rho-kinase activity is involved in the modulation of smooth muscle tone, especially during aberrant vascular contractions, such as coronary" ; ns1:mentions . _:b8584758 rdf:type ns1:Context ; rdf:value "is involved in the modulation of smooth muscle tone, especially during aberrant vascular contractions, such as coronary vasospasm, cerebral vasospasm after subarachnoid hemorrhage, and pulmonary hypertension [Shimokawa and Rashid, >>2007<<]. Recently, we found that Rho-kinase phosphorylates p190RhoGAP, one of the major negative regulators of Rho, and presumably inhibits its GAP activity in smooth muscle cells [Mori et al., 2009], which may form a positive feedback loop that" ; ns1:mentions . _:b8584759 rdf:type ns1:Context ; rdf:value "Recently, we found that Rho-kinase phosphorylates p190RhoGAP, one of the major negative regulators of Rho, and presumably inhibits its GAP activity in smooth muscle cells [Mori et al., >>2009<<], which may form a positive feedback loop that accounts for the hyperactivation of Rho at spastic sites." ; ns1:mentions . _:b8584760 rdf:type ns1:Context ; rdf:value "Stress fibers and focal adhesions confer contractility on a cell and are mediated by Rho/Rho-kinase signaling pathway [Amano et al., >>1997<<]. MLC phosphorylation which is necessary for the formation and maintenance of stress fibers and focal adhesions, is regulated by Rho-kinase and MLC phosphatase downstream of Rho, in cooperation with the Rho effector mDia [Watanabe et al.," ; ns1:mentions . _:b8584761 rdf:type ns1:Context ; rdf:value "phosphorylation which is necessary for the formation and maintenance of stress fibers and focal adhesions, is regulated by Rho-kinase and MLC phosphatase downstream of Rho, in cooperation with the Rho effector mDia [Watanabe et al., >>1999<<]. LIM kinases 1 and 2 are phosphorylated by Rho-kinase at Thr508 and Thr505, respectively, resulting in increased cofilin phosphorylation at Ser3 [Maekawa et al., 1999]." ; ns1:mentions . _:b8584762 rdf:type ns1:Context ; rdf:value "LIM kinases 1 and 2 are phosphorylated by Rho-kinase at Thr508 and Thr505, respectively, resulting in increased cofilin phosphorylation at Ser3 [Maekawa et al., >>1999<<]. Cofilin is an actin-depolymerizing factor and regulates actin dynamics, and its activity is inhibited by phosphorylation. Rho-kinase seems to induce and maintain stress fibers by increasing contractility via MLC phosphorylation and by" ; ns1:mentions . _:b8584763 rdf:type ns1:Context ; rdf:value "Isolated contractile stress fibers from fibroblasts contain Rho, Rho-kinase and MYPT1, and their contraction is sensitive to Rho-kinase inhibitors [Katoh et al., >>2001<<], suggesting that Rho, Rho-kinase and MLC phosphatase associate with microfilaments to form a modulatory apparatus for acto-myosin contraction." ; ns1:mentions . _:b8584764 rdf:type ns1:Context ; rdf:value "Rho family GTPases play critical roles in regulation of cell migration through their specific effectors [Etienne-Manneville and Hall, >>2002<<; Fukata et al., 2003]." ; ns1:mentions . _:b8584765 rdf:type ns1:Context ; rdf:value "Rho family GTPases play critical roles in regulation of cell migration through their specific effectors [Etienne-Manneville and Hall, 2002; Fukata et al., >>2003<<]." ; ns1:mentions . _:b8584766 rdf:type ns1:Context ; rdf:value "The roles of Rho/Rho-kinase in cell migration depend on the cell type and mode of migration [Nakayama et al., >>2005<<]. Inhibition of Rho or Rho-kinase results in the inhibition of migration through Boyden chambers, but not attachment, of monocytes [Worthylake et al., 2001], neutrophils, HL-60 [Hauert et al., 2002], eosinophils [Alblas et al., 2001], and" ; ns1:mentions . _:b8584767 rdf:type ns1:Context ; rdf:value "Inhibition of Rho or Rho-kinase results in the inhibition of migration through Boyden chambers, but not attachment, of monocytes [Worthylake et al., >>2001<<], neutrophils, HL-60 [Hauert et al., 2002], eosinophils [Alblas et al., 2001], and smooth muscle cells [Ai et al., 2001; Nishiguchi et al., 2003]." ; ns1:mentions . _:b8584768 rdf:type ns1:Context ; rdf:value "Inhibition of Rho or Rho-kinase results in the inhibition of migration through Boyden chambers, but not attachment, of monocytes [Worthylake et al., 2001], neutrophils, HL-60 [Hauert et al., >>2002<<], eosinophils [Alblas et al., 2001], and smooth muscle cells [Ai et al., 2001; Nishiguchi et al., 2003]." ; ns1:mentions . _:b8584769 rdf:type ns1:Context ; rdf:value "Inhibition of Rho or Rho-kinase results in the inhibition of migration through Boyden chambers, but not attachment, of monocytes [Worthylake et al., 2001], neutrophils, HL-60 [Hauert et al., 2002], eosinophils [Alblas et al., >>2001<<], and smooth muscle cells [Ai et al., 2001; Nishiguchi et al., 2003]." ; ns1:mentions . _:b8584770 rdf:type ns1:Context ; rdf:value "in the inhibition of migration through Boyden chambers, but not attachment, of monocytes [Worthylake et al., 2001], neutrophils, HL-60 [Hauert et al., 2002], eosinophils [Alblas et al., 2001], and smooth muscle cells [Ai et al., >>2001<<; Nishiguchi et al., 2003]." ; ns1:mentions . _:b8584771 rdf:type ns1:Context ; rdf:value "migration through Boyden chambers, but not attachment, of monocytes [Worthylake et al., 2001], neutrophils, HL-60 [Hauert et al., 2002], eosinophils [Alblas et al., 2001], and smooth muscle cells [Ai et al., 2001; Nishiguchi et al., >>2003<<]. Monocytes treated with Y-27632 or C3 exoenzyme (an inhibitor of Rho) have elongated tails, and cause a defect in tail detachment, and a mislocalizated integrins, the latter of which is not observed in cells treated with myosin" ; ns1:mentions . _:b8584772 rdf:type ns1:Context ; rdf:value "Y-27632 or C3 exoenzyme (an inhibitor of Rho) have elongated tails, and cause a defect in tail detachment, and a mislocalizated integrins, the latter of which is not observed in cells treated with myosin inhibitors [Worthylake et al., >>2001<<]. This suggests that not only myosin-mediated contraction but also integrin reorganization is necessary for the Rho/Rho-kinase-mediated tail retraction." ; ns1:mentions . _:b8584773 rdf:type ns1:Context ; rdf:value "fNLPNTL-induced neutrophil polarization is inhibited to some extent by treatment with Y-27632, whereas the number of non-polar cells with ruffles is increased [Hauert et al., >>2002<<]. Similar results have been shown for HL-60 cells stimulated with fMLP - the number of cells with flattened morphologies and multiple pseudopods is increased by the inhibition of Rho, Rho-kinase or myosin II [Xu et al., 2003]. In" ; ns1:mentions . _:b8584774 rdf:type ns1:Context ; rdf:value "Similar results have been shown for HL-60 cells stimulated with fMLP - the number of cells with flattened morphologies and multiple pseudopods is increased by the inhibition of Rho, Rho-kinase or myosin II [Xu et al., >>2003<<]. In Y-27632-treated HL-60 cells, the level of activated Rac is increased after stimulation with fMLP, suggesting that the multiple pseudopods observed after the inhibition of Rho/Rho-kinase are the consequence of aberrant activation of" ; ns1:mentions . _:b8584775 rdf:type ns1:Context ; rdf:value "The migration of fibroblasts during wound healing or random migration is not inhibited, but rather enhanced, by inhibition of Rho or Rho-kinase [Nobes and Hall, >>1999<<; Magdalena et al., 2003; Totsukawa et al., 2004]." ; ns1:mentions . _:b8584776 rdf:type ns1:Context ; rdf:value "The migration of fibroblasts during wound healing or random migration is not inhibited, but rather enhanced, by inhibition of Rho or Rho-kinase [Nobes and Hall, 1999; Magdalena et al., >>2003<<; Totsukawa et al., 2004]." ; ns1:mentions . _:b8584777 rdf:type ns1:Context ; rdf:value "The migration of fibroblasts during wound healing or random migration is not inhibited, but rather enhanced, by inhibition of Rho or Rho-kinase [Nobes and Hall, 1999; Magdalena et al., 2003; Totsukawa et al., >>2004<<]. In contrast to neutrorphils and HL-60 cells, Rho-kinase inhibition by Y-27632 leads to faster and straighter migration with a single leading edge and without Rac activation, whereas MLCK inhibition results in the formation of multiple" ; ns1:mentions . _:b8584778 rdf:type ns1:Context ; rdf:value "inhibition by Y-27632 leads to faster and straighter migration with a single leading edge and without Rac activation, whereas MLCK inhibition results in the formation of multiple protrusions in gerbil fibroma cells [Totsukawa et al., >>2004<<]." ; ns1:mentions . _:b8584779 rdf:type ns1:Context ; rdf:value "Furthermore, it has been shown that tumor cells use at least two types of migration in a three-dimensional matrix: Rho/Rho-kinase-dependent and Rac-dependent migration [Sahai and Marshall, >>2003<<]. Several tumor cell lines, such as A375 melanoma cell lines, can migrate through a 3D matrix in a Rac-dependent mesenchymal fashion or in a Rho/Rho-kinase-dependent amoeboid fashion." ; ns1:mentions . _:b8584780 rdf:type ns1:Context ; rdf:value "DOCK3 or Rac1 converts cells from the mesenchymal morphology to amoeboid one in a Rho-kinase/ARHGAP22 (RacGAP)-dependent manner, suggesting that these two types of migration are interconvertible and antagonistic [Sanz-Moreno et al., >>2008<<]." ; ns1:mentions . _:b8584781 rdf:type ns1:Context ; rdf:value "In neutrophils, PTEN is localized at the rear of cell and suppresses the production of PI(3,4,5)P3; the distribution of PTEN is under the control of Rho/Rho-kinase, most likely by the phosphorylation of PTEN by Rho-kinase [Li et al., >>2005<<]. We recently showed that Rho-kinase also phosphorylates PAR-3, a component of the PAR polarity complex, which leads to dissociation of PAR-3 from the PAR-6/aPKC complex [Nakayama et al., 2008]." ; ns1:mentions . _:b8584782 rdf:type ns1:Context ; rdf:value "We recently showed that Rho-kinase also phosphorylates PAR-3, a component of the PAR polarity complex, which leads to dissociation of PAR-3 from the PAR-6/aPKC complex [Nakayama et al., >>2008<<]. Because PAR-3 binds to the Rac GEF Tiam1/Tiam2 (STEF) and aPKC stimulates Rac GEF activity, Rho-kinase indirectly abrogates Rac activation by phosphorylating PAR-3. PAR-3 phosphorylation by Rho-kinase is observed not only at the rear of" ; ns1:mentions . _:b8584783 rdf:type ns1:Context ; rdf:value "CRMP-2 is phosphorylated by Rho-kinase at Thr555, which impairs its ability to bind to tubulin and numb [Arimura et al., >>2005<<]. Phosphorylation of CRMP-2 is increased by stimulation with LPA and ephrin-A5 in DRG and hippocampal neurons, respectively, and is implicated in growth cone collapse induced by these repulsive cues [Arimura et al., 2000; Arimura et al.," ; ns1:mentions . _:b8584784 rdf:type ns1:Context ; rdf:value "Phosphorylation of CRMP-2 is increased by stimulation with LPA and ephrin-A5 in DRG and hippocampal neurons, respectively, and is implicated in growth cone collapse induced by these repulsive cues [Arimura et al., >>2000<<; Arimura et al., 2005]." ; ns1:mentions . _:b8584785 rdf:type ns1:Context ; rdf:value "of CRMP-2 is increased by stimulation with LPA and ephrin-A5 in DRG and hippocampal neurons, respectively, and is implicated in growth cone collapse induced by these repulsive cues [Arimura et al., 2000; Arimura et al., >>2005<<]. MAP2, Tau, and neurofilament are also neuron-specific substrates for Rho-kinase, and their microtubule polymerizing activity and neurofilament assembly are inhibited by phosphorylation by Rho-kinase [Hashimoto et al., 1998; Amano et al." ; ns1:mentions . _:b8584786 rdf:type ns1:Context ; rdf:value "MAP2, Tau, and neurofilament are also neuron-specific substrates for Rho-kinase, and their microtubule polymerizing activity and neurofilament assembly are inhibited by phosphorylation by Rho-kinase [Hashimoto et al., >>1998<<; Amano et al., 2003]." ; ns1:mentions . _:b8584787 rdf:type ns1:Context ; rdf:value "Tau, and neurofilament are also neuron-specific substrates for Rho-kinase, and their microtubule polymerizing activity and neurofilament assembly are inhibited by phosphorylation by Rho-kinase [Hashimoto et al., 1998; Amano et al., >>2003<<]. Phosphorylation of MAP2/Tau and neurofilament may prevent neurite elongation and shorten neurites by destabilizing microtubules and intermediate filaments." ; ns1:mentions . _:b8584788 rdf:type ns1:Context ; rdf:value "The control of cellular contraction through MYPT1/MLC phosphorylation by Rho-kinase is also thought to participate in neurite retraction and inhibition of neurite outgrowth [Amano et al., >>1998<<; Hirose et al., 1998]." ; ns1:mentions . _:b8584789 rdf:type ns1:Context ; rdf:value "The control of cellular contraction through MYPT1/MLC phosphorylation by Rho-kinase is also thought to participate in neurite retraction and inhibition of neurite outgrowth [Amano et al., 1998; Hirose et al., >>1998<<]. LIMK1/cofilin has also been implicated in regulation of growth cone morphology in chick DRG neurons [Endo et al., 2003], potentially downstream of Rho-kinase." ; ns1:mentions . _:b8584790 rdf:type ns1:Context ; rdf:value "LIMK1/cofilin has also been implicated in regulation of growth cone morphology in chick DRG neurons [Endo et al., >>2003<<], potentially downstream of Rho-kinase." ; ns1:mentions . _:b8584791 rdf:type ns1:Context ; rdf:value "cultured cerebellar granule neurons with Y-27632 triggered immediate neurite outgrowth at an early stage, though it was less effective at later stages, suggesting that Rho-kinase controls the initiation of axonogenesis [Bito et al., >>2000<<]. At the neuronal maturation stage, dendritic branching and spine formation are markedly inhibited when constitutively activated RhoA is expressed in hippocampal slice cultures; this effect can be abrogated by the administration of" ; ns1:mentions . _:b8584792 rdf:type ns1:Context ; rdf:value "stage, dendritic branching and spine formation are markedly inhibited when constitutively activated RhoA is expressed in hippocampal slice cultures; this effect can be abrogated by the administration of Y-27632 [Nakayama et al., >>2000<<], implying that Rho-kinase plays a role in dendrite formation." ; ns1:mentions . _:b8584793 rdf:type ns1:Context ; rdf:value "CRMP-2 is phosphorylated at Thr555 following treatment with MAG or Nogo, and overexpression of CRMP-2 causes neurite extension in the presence of MAG [Mimura et al., >>2006<<]." ; ns1:mentions . _:b8584794 rdf:type ns1:Context ; rdf:value "Rho-kinase inhibitors also show a potential protective effects in Alzheimer's disease [Tang and Liou, >>2007<<]. Alzheimer's disease is characterized by extracellular amyloid aggregates of toxic 40- or 42-amino-acid long amyloid-\u03B2 (A\u03B240 or A\u03B242) peptides, which are generated from amyloid precursor protein (APP) that is abnormally cleaved by \u03B1- and" ; ns1:mentions . _:b8584795 rdf:type ns1:Context ; rdf:value "Treatment with Y-27632 decreased the production of A\u03B242 in SH-SY5Y cells expressing mutant APP (APPswe) and in model mice [Zhou et al., >>2003<<]. Shedding of APP, which determines the alternative forms, soluble APP (sAPP) and toxic A\u03B242, was also found to be modulated by Rho-kinase in APPswe-expressing N2a cells [Pedrini et al., 2005]." ; ns1:mentions . _:b8584796 rdf:type ns1:Context ; rdf:value "Shedding of APP, which determines the alternative forms, soluble APP (sAPP) and toxic A\u03B242, was also found to be modulated by Rho-kinase in APPswe-expressing N2a cells [Pedrini et al., >>2005<<]." ; ns1:mentions . _:b8584797 rdf:type ns1:Context ; rdf:value "In addition to Rho, Plk1 has also been found to associate with and activate Rho-kinase synergistically with Rho during cytokinesis [Lowery et al., >>2007<<]. Rho and Rho-kinase are involved in both the progression of the cleavage furrow formation and the disassembly of intermediate filaments beneath cleavage furrow [Matsumura, 2005] [Izawa and Inagaki, 2006]. Rho-kinase regulates MLC" ; ns1:mentions . _:b8584798 rdf:type ns1:Context ; rdf:value "Rho and Rho-kinase are involved in both the progression of the cleavage furrow formation and the disassembly of intermediate filaments beneath cleavage furrow [Matsumura, >>2005<<] [Izawa and Inagaki, 2006]." ; ns1:mentions . _:b8584799 rdf:type ns1:Context ; rdf:value "Rho and Rho-kinase are involved in both the progression of the cleavage furrow formation and the disassembly of intermediate filaments beneath cleavage furrow [Matsumura, 2005] [Izawa and Inagaki, >>2006<<]. Rho-kinase regulates MLC phosphorylation through MLC phosphatase, and possibly by direct phosphorylation, at the contractile ring. At the same time, Rho-kinase phosphorylates the head domain of intermediate filaments, such as vimentin," ; ns1:mentions . _:b8584800 rdf:type ns1:Context ; rdf:value "Inhibition of Rho-kinase by Y-27632 does not completely arrest cytokinesis in cultured cells, though it does induce some abnormalites and delays in cleavage [Kosako et al., >>2000<<]. Various other kinases, such as Aurora-B and Citron-kinase, seem to play redundant roles in cytokinesis." ; ns1:mentions . _:b8584801 rdf:type ns1:Context ; rdf:value "as Rho-kinase substrates that are phosphorylated at Thr567, Thr564, and Thr558, respectively; phosphorylation of ERM proteins by Rho-kinase maintains their activity by crosslinking transmembrane proteins to F-actin [Fukata et al., >>1998<<; Matsui et al., 1998]." ; ns1:mentions . _:b8584802 rdf:type ns1:Context ; rdf:value "that are phosphorylated at Thr567, Thr564, and Thr558, respectively; phosphorylation of ERM proteins by Rho-kinase maintains their activity by crosslinking transmembrane proteins to F-actin [Fukata et al., 1998; Matsui et al., >>1998<<]. PKC and MRCK were also demonstrated to phosphorylate ERM at these sites, and the contribution of Rho-kinase to ERM phosphorylation is thought to depend on the cell type and situation, such as in smooth muscle cells upon static pressure" ; ns1:mentions . _:b8584803 rdf:type ns1:Context ; rdf:value "also demonstrated to phosphorylate ERM at these sites, and the contribution of Rho-kinase to ERM phosphorylation is thought to depend on the cell type and situation, such as in smooth muscle cells upon static pressure [Onoue et al., >>2008<<], in hippocampal neurons upon glutamate stimulation [Jeon et al., 2002], in T cells from systemic lupus erythematosus patients [Li et al., 2007], and in Jurkat cells upon Fas ligand stimulation [Hebert et al., 2008]." ; ns1:mentions . _:b8584804 rdf:type ns1:Context ; rdf:value "of Rho-kinase to ERM phosphorylation is thought to depend on the cell type and situation, such as in smooth muscle cells upon static pressure [Onoue et al., 2008], in hippocampal neurons upon glutamate stimulation [Jeon et al., >>2002<<], in T cells from systemic lupus erythematosus patients [Li et al., 2007], and in Jurkat cells upon Fas ligand stimulation [Hebert et al., 2008]." ; ns1:mentions . _:b8584805 rdf:type ns1:Context ; rdf:value "type and situation, such as in smooth muscle cells upon static pressure [Onoue et al., 2008], in hippocampal neurons upon glutamate stimulation [Jeon et al., 2002], in T cells from systemic lupus erythematosus patients [Li et al., >>2007<<], and in Jurkat cells upon Fas ligand stimulation [Hebert et al., 2008]." ; ns1:mentions . _:b8584806 rdf:type ns1:Context ; rdf:value "[Onoue et al., 2008], in hippocampal neurons upon glutamate stimulation [Jeon et al., 2002], in T cells from systemic lupus erythematosus patients [Li et al., 2007], and in Jurkat cells upon Fas ligand stimulation [Hebert et al., >>2008<<]." ; ns1:mentions . _:b8584807 rdf:type ns1:Context ; rdf:value "Rho-kinase is also localized in the nucleus and interacts with p300 acetyltransferase, which forms a large nuclear protein complex [Tanaka et al., >>2006<<]. Rho-kinase phosphorylates p300 and activates its acetyltransferase activity, in vitro and in vivo, resulting in the enhancement of p300-dependent transcription in U205 cells [Tanaka et al., 2006]." ; ns1:mentions . _:b8584808 rdf:type ns1:Context ; rdf:value "Rho-kinase phosphorylates p300 and activates its acetyltransferase activity, in vitro and in vivo, resulting in the enhancement of p300-dependent transcription in U205 cells [Tanaka et al., >>2006<<]." ; ns1:mentions . _:b8584809 rdf:type ns1:Context ; rdf:value "Rho/Rho-kinase has been demonstrated to be involved in planar polarity establishment downstream of the Wnt/Frizzled/Dishevelled pathway in Drosophila eye and wing development [Winter et al., >>2001<<] and in zebrafish gastrulation convergence and extension [Marlow et al., 2002]." ; ns1:mentions . _:b8584810 rdf:type ns1:Context ; rdf:value "to be involved in planar polarity establishment downstream of the Wnt/Frizzled/Dishevelled pathway in Drosophila eye and wing development [Winter et al., 2001] and in zebrafish gastrulation convergence and extension [Marlow et al., >>2002<<]. Nucleophosmin (NPM)/B23 is a centrosomal protein that is reported to associate with Rho-kinase at the centrosome [Ma et al., 2006]." ; ns1:mentions . _:b8584811 rdf:type ns1:Context ; rdf:value "Nucleophosmin (NPM)/B23 is a centrosomal protein that is reported to associate with Rho-kinase at the centrosome [Ma et al., >>2006<<]. NPM activates Rho-kinase in a phosphorylation state-dependent manner by CDK2/cyclin E, which is involved in preventing centrosome reduplication [Ma et al., 2006]. Several lines of evidence suggest that the Rho-kinase signaling pathway" ; ns1:mentions . _:b8584812 rdf:type ns1:Context ; rdf:value "NPM activates Rho-kinase in a phosphorylation state-dependent manner by CDK2/cyclin E, which is involved in preventing centrosome reduplication [Ma et al., >>2006<<]. Several lines of evidence suggest that the Rho-kinase signaling pathway also modulates cell survival and apoptosis, as Rho-kinase is known to be involved in morphological changes that occur during apoptosis [Coleman et al., 2001;" ; ns1:mentions . _:b8584813 rdf:type ns1:Context ; rdf:value "Several lines of evidence suggest that the Rho-kinase signaling pathway also modulates cell survival and apoptosis, as Rho-kinase is known to be involved in morphological changes that occur during apoptosis [Coleman et al., >>2001<<; Sebbagh et al., 2001; Sebbagh et al., 2005]." ; ns1:mentions . _:b8584814 rdf:type ns1:Context ; rdf:value "of evidence suggest that the Rho-kinase signaling pathway also modulates cell survival and apoptosis, as Rho-kinase is known to be involved in morphological changes that occur during apoptosis [Coleman et al., 2001; Sebbagh et al., >>2001<<; Sebbagh et al., 2005]. Recently, Rho-kinase inhibitors such as Y-27632 have been shown to have protective effects on human embryonic stem cells." ; ns1:mentions . _:b8584815 rdf:type ns1:Context ; rdf:value "that the Rho-kinase signaling pathway also modulates cell survival and apoptosis, as Rho-kinase is known to be involved in morphological changes that occur during apoptosis [Coleman et al., 2001; Sebbagh et al., 2001; Sebbagh et al., >>2005<<]. Recently, Rho-kinase inhibitors such as Y-27632 have been shown to have protective effects on human embryonic stem cells." ; ns1:mentions . _:b8584816 rdf:type ns1:Context ; rdf:value "Administration of Y-27632 prevents apoptosis and enhances survival of human embryonic stem cells at low culture density [Watanabe et al., >>2007<<], possibly through the regulation of MLC phosphorylation and cell-cell interactions [Harb et al., 2008]." ; ns1:mentions . _:b8584817 rdf:type ns1:Context ; rdf:value "of Y-27632 prevents apoptosis and enhances survival of human embryonic stem cells at low culture density [Watanabe et al., 2007], possibly through the regulation of MLC phosphorylation and cell-cell interactions [Harb et al., >>2008<<]. However, inhibition of Rho-kinase activity can promote apoptosis in certain situations [Shibata et al., 2003; Svoboda et al., 2004; Moore et al., 2004] and enhances cytotoxic polyglutamate (polyQ) aggregates of huntingtin, androgen" ; ns1:mentions . _:b8584818 rdf:type ns1:Context ; rdf:value "However, inhibition of Rho-kinase activity can promote apoptosis in certain situations [Shibata et al., >>2003<<; Svoboda et al., 2004; Moore et al., 2004] and enhances cytotoxic polyglutamate (polyQ) aggregates of huntingtin, androgen receptor, ataxin-2, and atropin-1 [Shao et al., 2008; Bauer et al., 2009]." ; ns1:mentions . _:b8584819 rdf:type ns1:Context ; rdf:value "However, inhibition of Rho-kinase activity can promote apoptosis in certain situations [Shibata et al., 2003; Svoboda et al., >>2004<<; Moore et al., 2004] and enhances cytotoxic polyglutamate (polyQ) aggregates of huntingtin, androgen receptor, ataxin-2, and atropin-1 [Shao et al., 2008; Bauer et al., 2009]." ; ns1:mentions . _:b8584820 rdf:type ns1:Context ; rdf:value "However, inhibition of Rho-kinase activity can promote apoptosis in certain situations [Shibata et al., 2003; Svoboda et al., 2004; Moore et al., >>2004<<] and enhances cytotoxic polyglutamate (polyQ) aggregates of huntingtin, androgen receptor, ataxin-2, and atropin-1 [Shao et al., 2008; Bauer et al., 2009]." ; ns1:mentions . _:b8584821 rdf:type ns1:Context ; rdf:value "promote apoptosis in certain situations [Shibata et al., 2003; Svoboda et al., 2004; Moore et al., 2004] and enhances cytotoxic polyglutamate (polyQ) aggregates of huntingtin, androgen receptor, ataxin-2, and atropin-1 [Shao et al., >>2008<<; Bauer et al., 2009]." ; ns1:mentions . _:b8584822 rdf:type ns1:Context ; rdf:value "in certain situations [Shibata et al., 2003; Svoboda et al., 2004; Moore et al., 2004] and enhances cytotoxic polyglutamate (polyQ) aggregates of huntingtin, androgen receptor, ataxin-2, and atropin-1 [Shao et al., 2008; Bauer et al., >>2009<<]." ; ns1:mentions . _:b8584823 rdf:type ns1:Context ; rdf:value "We have recently identified more than 100 potential substrates of Rho-kinase by the interactome approach, using the catalytic domain of Rho-kinase, and have isolated novel substrates such as Doublecortin, AP180 and APP [Amano et al., >>2010<<]. Rho-kinase contributes to complicated intracellular signaling networks in a wide range of situations, and further analysis will shed light on its biological mechanisms and potential therapeutics for the disease treatment." ; ns1:mentions . _:b441723204 rdf:type ns1:RelevantBibliographicResource . @prefix xsd: . _:b441723204 ns1:RelevantScore "22"^^xsd:nonNegativeInteger ; ns1:hasRelevantPaperId . _:b441723205 rdf:type ns1:RelevantBibliographicResource ; ns1:RelevantScore "19"^^xsd:nonNegativeInteger ; ns1:hasRelevantPaperId . _:b441723206 rdf:type ns1:RelevantBibliographicResource ; ns1:RelevantScore "19"^^xsd:nonNegativeInteger ; ns1:hasRelevantPaperId . _:b441723207 rdf:type ns1:RelevantBibliographicResource ; ns1:RelevantScore "17"^^xsd:nonNegativeInteger ; ns1:hasRelevantPaperId . _:b441723208 rdf:type ns1:RelevantBibliographicResource ; ns1:RelevantScore "15"^^xsd:nonNegativeInteger ; ns1:hasRelevantPaperId . _:b441723209 rdf:type ns1:RelevantBibliographicResource ; ns1:RelevantScore "15"^^xsd:nonNegativeInteger ; 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