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bibo:doi: 10.1083%2Fjcb.200311031
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Subject Item: _:vb803944
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dc:title: introduction
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Subject Item: _:vb803945
rdf:type: n3:Context
rdf:value: Their plasma membranes are subdivided into apical and basolateral domains that are separated by specialized junctional structures, such as tight junctions (TJ) and the zonula adherens (ZA; for reviews see Drubin and Nelson, >>1996<<; Müller, 2000; Tepass et al., 2001; Roh and Margolis, 2003).
n3:mentions: n4:8608587

Subject Item: _:vb803946
rdf:type: n3:Context
rdf:value: plasma membranes are subdivided into apical and basolateral domains that are separated by specialized junctional structures, such as tight junctions (TJ) and the zonula adherens (ZA; for reviews see Drubin and Nelson, 1996; Müller, >>2000<<; Tepass et al., 2001; Roh and Margolis, 2003).
n3:mentions: n4:10822259

Subject Item: _:vb803947
rdf:type: n3:Context
rdf:value: subdivided into apical and basolateral domains that are separated by specialized junctional structures, such as tight junctions (TJ) and the zonula adherens (ZA; for reviews see Drubin and Nelson, 1996; Müller, 2000; Tepass et al., >>2001<<; Roh and Margolis, 2003).
n3:mentions: n4:11700298

Subject Item: _:vb803948
rdf:type: n3:Context
rdf:value: and basolateral domains that are separated by specialized junctional structures, such as tight junctions (TJ) and the zonula adherens (ZA; for reviews see Drubin and Nelson, 1996; Müller, 2000; Tepass et al., 2001; Roh and Margolis, >>2003<<). Formation and stabilization of these junctions are paramount for the maintenance of epithelial polarity, which, in turn, is required for proper epithelial cell physiology, cell motility, asymmetric division, and intercellular signaling
n3:mentions: n4:12890661

Subject Item: _:vb803949
rdf:type: n3:Context
rdf:value: junctions are paramount for the maintenance of epithelial polarity, which, in turn, is required for proper epithelial cell physiology, cell motility, asymmetric division, and intercellular signaling (for review see Tepass et al., >>2001<<). Hence, the functional analysis of the factors that establish and/or maintain epithelial polarity is a major issue in developmental biology.
n3:mentions: n4:11700298

Subject Item: _:vb803950
rdf:type: n3:Context
rdf:value: Thus, three membrane-associated multiprotein complexes, the Bazooka (Baz), Crumbs, and Discs large (Dlg) complexes, are required to organize apicobasal polarity in the epithelial cells of the Drosophila embryo (for reviews see Müller, >>2000<<; Ohno, 2001; Tepass et al., 2001; Knust and Bossinger, 2002; Henrique and Schweisguth, 2003; Roh and Margolis, 2003).
n3:mentions: n4:10822259

Subject Item: _:vb803951
rdf:type: n3:Context
rdf:value: membrane-associated multiprotein complexes, the Bazooka (Baz), Crumbs, and Discs large (Dlg) complexes, are required to organize apicobasal polarity in the epithelial cells of the Drosophila embryo (for reviews see Müller, 2000; Ohno, >>2001<<; Tepass et al., 2001; Knust and Bossinger, 2002; Henrique and Schweisguth, 2003; Roh and Margolis, 2003).
n3:mentions: n4:11544035

Subject Item: _:vb803952
rdf:type: n3:Context
rdf:value: complexes, the Bazooka (Baz), Crumbs, and Discs large (Dlg) complexes, are required to organize apicobasal polarity in the epithelial cells of the Drosophila embryo (for reviews see Müller, 2000; Ohno, 2001; Tepass et al., >>2001<<; Knust and Bossinger, 2002; Henrique and Schweisguth, 2003; Roh and Margolis, 2003).
n3:mentions: n4:11700298

Subject Item: _:vb803953
rdf:type: n3:Context
rdf:value: Bazooka (Baz), Crumbs, and Discs large (Dlg) complexes, are required to organize apicobasal polarity in the epithelial cells of the Drosophila embryo (for reviews see Müller, 2000; Ohno, 2001; Tepass et al., 2001; Knust and Bossinger, >>2002<<; Henrique and Schweisguth, 2003; Roh and Margolis, 2003).
n3:mentions: n4:12471248

Subject Item: _:vb803954
rdf:type: n3:Context
rdf:value: large (Dlg) complexes, are required to organize apicobasal polarity in the epithelial cells of the Drosophila embryo (for reviews see Müller, 2000; Ohno, 2001; Tepass et al., 2001; Knust and Bossinger, 2002; Henrique and Schweisguth, >>2003<<; Roh and Margolis, 2003).
n3:mentions: n4:12888006

Subject Item: _:vb803955
rdf:type: n3:Context
rdf:value: are required to organize apicobasal polarity in the epithelial cells of the Drosophila embryo (for reviews see Müller, 2000; Ohno, 2001; Tepass et al., 2001; Knust and Bossinger, 2002; Henrique and Schweisguth, 2003; Roh and Margolis, >>2003<<). The Baz complex is formed by the PSD-95/Dlg/ZO-1 domain containing proteins Baz and DPar-6, and the Drosophila atypical PKC (DaPKC), a Ser/Thr kinase (Kuchinke et al., 1998; Wodarz et al., 2000; Petronczki and Knoblich, 2001).
n3:mentions: n4:12890661

Subject Item: _:vb803956
rdf:type: n3:Context
rdf:value: The Baz complex is formed by the PSD-95/Dlg/ZO-1 domain containing proteins Baz and DPar-6, and the Drosophila atypical PKC (DaPKC), a Ser/Thr kinase (Kuchinke et al., >>1998<<; Wodarz et al., 2000; Petronczki and Knoblich, 2001).
n3:mentions: n4:9889099

Subject Item: _:vb803957
rdf:type: n3:Context
rdf:value: The Baz complex is formed by the PSD-95/Dlg/ZO-1 domain containing proteins Baz and DPar-6, and the Drosophila atypical PKC (DaPKC), a Ser/Thr kinase (Kuchinke et al., 1998; Wodarz et al., >>2000<<; Petronczki and Knoblich, 2001).
n3:mentions: n4:10995441

Subject Item: _:vb803958
rdf:type: n3:Context
rdf:value: The Baz complex is formed by the PSD-95/Dlg/ZO-1 domain containing proteins Baz and DPar-6, and the Drosophila atypical PKC (DaPKC), a Ser/Thr kinase (Kuchinke et al., 1998; Wodarz et al., 2000; Petronczki and Knoblich, >>2001<<). This complex, which is localized at the marginal zone of the apico-lateral cell membrane, above the ZA, is formed stepwise during early embryogenesis. Thus, at blastoderm stage, Baz and DaPKC are found at the apical membrane domain
n3:mentions: n4:11146625

Subject Item: _:vb803959
rdf:type: n3:Context
rdf:value: Thus, at blastoderm stage, Baz and DaPKC are found at the apical membrane domain (Wodarz et al., >>2000<<; Bilder et al., 2003).
n3:mentions: n4:10995441

Subject Item: _:vb803960
rdf:type: n3:Context
rdf:value: Thus, at blastoderm stage, Baz and DaPKC are found at the apical membrane domain (Wodarz et al., 2000; Bilder et al., >>2003<<). Slightly later, at the onset of gastrulation, DPar-6 is incorporated to the Baz–DaPKC complex, where it binds directly to both Baz and DaPKC (Petronczki and Knoblich, 2001). Embryos deficient in Baz or DPar-6 cannot properly assemble
n3:mentions: n4:12510194

Subject Item: _:vb803961
rdf:type: n3:Context
rdf:value: Slightly later, at the onset of gastrulation, DPar-6 is incorporated to the Baz–DaPKC complex, where it binds directly to both Baz and DaPKC (Petronczki and Knoblich, >>2001<<). Embryos deficient in Baz or DPar-6 cannot properly assemble the ZA and lack several apical markers of the cell membrane (Müller and Wieschaus, 1996; Petronczki and Knoblich, 2001). Similarly, epithelial cells of DaPKC mutant imaginal
n3:mentions: n4:11146625

Subject Item: _:vb803962
rdf:type: n3:Context
rdf:value: Embryos deficient in Baz or DPar-6 cannot properly assemble the ZA and lack several apical markers of the cell membrane (Müller and Wieschaus, >>1996<<; Petronczki and Knoblich, 2001).
n3:mentions: n4:8698811

Subject Item: _:vb803963
rdf:type: n3:Context
rdf:value: Embryos deficient in Baz or DPar-6 cannot properly assemble the ZA and lack several apical markers of the cell membrane (Müller and Wieschaus, 1996; Petronczki and Knoblich, >>2001<<). Similarly, epithelial cells of DaPKC mutant imaginal discs display disrupted apicobasal polarity (Rolls et al., 2003). Thus, each of the components of the Baz complex is essential to establish epithelial polarity.
n3:mentions: n4:11146625

Subject Item: _:vb803964
rdf:type: n3:Context
rdf:value: Similarly, epithelial cells of DaPKC mutant imaginal discs display disrupted apicobasal polarity (Rolls et al., >>2003<<). Thus, each of the components of the Baz complex is essential to establish epithelial polarity.
n3:mentions: n4:14657233

Subject Item: _:vb803965
rdf:type: n3:Context
rdf:value: It consists of the transmembrane (TM) protein Crumbs (Crb) and the cytoplasmic PDZ-containing proteins Stardust (Sdt) and Pals1-associated TJ protein (Patj; formerly known as Discs lost; Tepass et al., >>1990<<; Bhat et al., 1999; Bachmann et al., 2001; Hong et al., 2001; Pielage et al., 2003).
n3:mentions: n4:2344615

Subject Item: _:vb803966
rdf:type: n3:Context
rdf:value: It consists of the transmembrane (TM) protein Crumbs (Crb) and the cytoplasmic PDZ-containing proteins Stardust (Sdt) and Pals1-associated TJ protein (Patj; formerly known as Discs lost; Tepass et al., 1990; Bhat et al., >>1999<<; Bachmann et al., 2001; Hong et al., 2001; Pielage et al., 2003).
n3:mentions: n4:10102271

Subject Item: _:vb803967
rdf:type: n3:Context
rdf:value: of the transmembrane (TM) protein Crumbs (Crb) and the cytoplasmic PDZ-containing proteins Stardust (Sdt) and Pals1-associated TJ protein (Patj; formerly known as Discs lost; Tepass et al., 1990; Bhat et al., 1999; Bachmann et al., >>2001<<; Hong et al., 2001; Pielage et al., 2003). Crb contains 30 epidermal growth factor–like and four laminin A G-domain–like repeats in its extracellular region and a short intracellular domain (Tepass et al., 1990).
n3:mentions: n4:11740560

Subject Item: _:vb803968
rdf:type: n3:Context
rdf:value: (TM) protein Crumbs (Crb) and the cytoplasmic PDZ-containing proteins Stardust (Sdt) and Pals1-associated TJ protein (Patj; formerly known as Discs lost; Tepass et al., 1990; Bhat et al., 1999; Bachmann et al., 2001; Hong et al., >>2001<<; Pielage et al., 2003). Crb contains 30 epidermal growth factor–like and four laminin A G-domain–like repeats in its extracellular region and a short intracellular domain (Tepass et al., 1990).
n3:mentions: n4:11740559

Subject Item: _:vb803969
rdf:type: n3:Context
rdf:value: (Crb) and the cytoplasmic PDZ-containing proteins Stardust (Sdt) and Pals1-associated TJ protein (Patj; formerly known as Discs lost; Tepass et al., 1990; Bhat et al., 1999; Bachmann et al., 2001; Hong et al., 2001; Pielage et al., >>2003<<). Crb contains 30 epidermal growth factor–like and four laminin A G-domain–like repeats in its extracellular region and a short intracellular domain (Tepass et al., 1990).
n3:mentions: n4:14667407

Subject Item: _:vb803970
rdf:type: n3:Context
rdf:value: Crb contains 30 epidermal growth factor–like and four laminin A G-domain–like repeats in its extracellular region and a short intracellular domain (Tepass et al., >>1990<<). Expression of this intracellular domain partially normalizes mutant crb embryos (Wodarz et al., 1995; Klebes and Knust, 2000). This suggests that Crb exerts its function, at least in part, by protein–protein interactions mediated by
n3:mentions: n4:2344615

Subject Item: _:vb803971
rdf:type: n3:Context
rdf:value: Expression of this intracellular domain partially normalizes mutant crb embryos (Wodarz et al., >>1995<<; Klebes and Knust, 2000).
n3:mentions: n4:7606787

Subject Item: _:vb803972
rdf:type: n3:Context
rdf:value: Expression of this intracellular domain partially normalizes mutant crb embryos (Wodarz et al., 1995; Klebes and Knust, >>2000<<). This suggests that Crb exerts its function, at least in part, by protein–protein interactions mediated by this domain. The intracellular domain has been subdivided into proximal juxtamembrane and COOH-terminal subdomains. The latter
n3:mentions: n4:10662667

Subject Item: _:vb803973
rdf:type: n3:Context
rdf:value: The latter contains the binding site for Sdt (Bachmann et al., >>2001<<; Hong et al., 2001; Roh et al., 2002), which on its turn binds to Patj (Roh et al., 2002).
n3:mentions: n4:11740560

Subject Item: _:vb803974
rdf:type: n3:Context
rdf:value: The latter contains the binding site for Sdt (Bachmann et al., 2001; Hong et al., >>2001<<; Roh et al., 2002), which on its turn binds to Patj (Roh et al., 2002).
n3:mentions: n4:11740559

Subject Item: _:vb803975
rdf:type: n3:Context
rdf:value: The latter contains the binding site for Sdt (Bachmann et al., 2001; Hong et al., 2001; Roh et al., >>2002<<), which on its turn binds to Patj (Roh et al., 2002).
n3:mentions: n4:11927608

Subject Item: _:vb803976
rdf:type: n3:Context
rdf:value: The latter contains the binding site for Sdt (Bachmann et al., 2001; Hong et al., 2001; Roh et al., 2002), which on its turn binds to Patj (Roh et al., >>2002<<). The juxtamembrane domain is required for Crb to form a complex with DMoesin and β-heavy spectrin and thus mediates the interaction of the Crb complex with the apical spectrin cytoskeleton (Medina et al., 2002). Genetic studies have
n3:mentions: n4:11927608

Subject Item: _:vb803977
rdf:type: n3:Context
rdf:value: The juxtamembrane domain is required for Crb to form a complex with DMoesin and β-heavy spectrin and thus mediates the interaction of the Crb complex with the apical spectrin cytoskeleton (Medina et al., >>2002<<). Genetic studies have shown that the Crb complex is, similarly to the Baz complex, indispensable for the establishment of epithelial apicobasal polarity and stabilization of the ZA (Knust et al., 1993; Grawe et al., 1996; Müller and
n3:mentions: n4:12213838

Subject Item: _:vb803978
rdf:type: n3:Context
rdf:value: Genetic studies have shown that the Crb complex is, similarly to the Baz complex, indispensable for the establishment of epithelial apicobasal polarity and stabilization of the ZA (Knust et al., 1993; Grawe et al., >>1996<<; Müller and Wieschaus, 1996; Tepass, 1996; Bachmann et al., 2001; Hong et al., 2001).
n3:mentions: n4:8631272

Subject Item: _:vb803979
rdf:type: n3:Context
rdf:value: studies have shown that the Crb complex is, similarly to the Baz complex, indispensable for the establishment of epithelial apicobasal polarity and stabilization of the ZA (Knust et al., 1993; Grawe et al., 1996; Müller and Wieschaus, >>1996<<; Tepass, 1996; Bachmann et al., 2001; Hong et al., 2001).
n3:mentions: n4:8698811

Subject Item: _:vb803980
rdf:type: n3:Context
rdf:value: that the Crb complex is, similarly to the Baz complex, indispensable for the establishment of epithelial apicobasal polarity and stabilization of the ZA (Knust et al., 1993; Grawe et al., 1996; Müller and Wieschaus, 1996; Tepass, >>1996<<; Bachmann et al., 2001; Hong et al., 2001).
n3:mentions: n4:8660889

Subject Item: _:vb803981
rdf:type: n3:Context
rdf:value: is, similarly to the Baz complex, indispensable for the establishment of epithelial apicobasal polarity and stabilization of the ZA (Knust et al., 1993; Grawe et al., 1996; Müller and Wieschaus, 1996; Tepass, 1996; Bachmann et al., >>2001<<; Hong et al., 2001).
n3:mentions: n4:11740560

Subject Item: _:vb803982
rdf:type: n3:Context
rdf:value: the Baz complex, indispensable for the establishment of epithelial apicobasal polarity and stabilization of the ZA (Knust et al., 1993; Grawe et al., 1996; Müller and Wieschaus, 1996; Tepass, 1996; Bachmann et al., 2001; Hong et al., >>2001<<).
n3:mentions: n4:11740559

Subject Item: _:vb803983
rdf:type: n3:Context
rdf:value: The third complex, formed by the PDZ proteins Dlg (Woods and Bryant, >>1991<<) and Scribble (Scrib; Bilder and Perrimon, 2000), and the Myosin type II binding protein Lethal giant larvae (Lgl; Mechler et al., 1985), is found at the basolateral domain of the cell membrane, basal to the ZA.
n3:mentions: n4:1651169

Subject Item: _:vb803984
rdf:type: n3:Context
rdf:value: The third complex, formed by the PDZ proteins Dlg (Woods and Bryant, 1991) and Scribble (Scrib; Bilder and Perrimon, >>2000<<), and the Myosin type II binding protein Lethal giant larvae (Lgl; Mechler et al., 1985), is found at the basolateral domain of the cell membrane, basal to the ZA.
n3:mentions: n4:10688207

Subject Item: _:vb803985
rdf:type: n3:Context
rdf:value: The third complex, formed by the PDZ proteins Dlg (Woods and Bryant, 1991) and Scribble (Scrib; Bilder and Perrimon, 2000), and the Myosin type II binding protein Lethal giant larvae (Lgl; Mechler et al., >>1985<<), is found at the basolateral domain of the cell membrane, basal to the ZA.
n3:mentions: n4:3928370

Subject Item: _:vb803986
rdf:type: n3:Context
rdf:value: These proteins are required to restrict the Baz and Crb complexes to the apical cell membrane and for correct positioning of the ZA (Bilder et al., >>2000<<, 2003; Bilder and Perrimon, 2000; Tanentzapf and Tepass, 2003).
n3:mentions: n4:10884224

Subject Item: _:vb803987
rdf:type: n3:Context
rdf:value: These proteins are required to restrict the Baz and Crb complexes to the apical cell membrane and for correct positioning of the ZA (Bilder et al., 2000, >>2003<<; Bilder and Perrimon, 2000; Tanentzapf and Tepass, 2003).
n3:mentions: n4:12510194

Subject Item: _:vb803988
rdf:type: n3:Context
rdf:value: These proteins are required to restrict the Baz and Crb complexes to the apical cell membrane and for correct positioning of the ZA (Bilder et al., 2000, 2003; Bilder and Perrimon, >>2000<<; Tanentzapf and Tepass, 2003).
n3:mentions: n4:10688207

Subject Item: _:vb803989
rdf:type: n3:Context
rdf:value: These proteins are required to restrict the Baz and Crb complexes to the apical cell membrane and for correct positioning of the ZA (Bilder et al., 2000, 2003; Bilder and Perrimon, 2000; Tanentzapf and Tepass, >>2003<<).
n3:mentions: n4:12510193

Subject Item: _:vb803990
rdf:type: n3:Context
rdf:value: The three polarity complexes are evolutionarily conserved (for reviews see Ohno, >>2001<<; Roh and Margolis, 2003; Macara, 2004).
n3:mentions: n4:11544035

Subject Item: _:vb803991
rdf:type: n3:Context
rdf:value: The three polarity complexes are evolutionarily conserved (for reviews see Ohno, 2001; Roh and Margolis, >>2003<<; Macara, 2004).
n3:mentions: n4:12890661

Subject Item: _:vb803992
rdf:type: n3:Context
rdf:value: The three polarity complexes are evolutionarily conserved (for reviews see Ohno, 2001; Roh and Margolis, 2003; Macara, >>2004<<). Thus, in mammalian epithelial cells, the homologues of DaPKC, Baz, and DPar-6, namely aPKC, Par-3/atypical PKC isotype-specific interacting protein (ASIP), and Par-6, and the corresponding homologues of Crb, Sdt, and Patj, that is,
n3:mentions: n4:14991002

Subject Item: _:vb803993
rdf:type: n3:Context
rdf:value: The basolateral proteins Scrib, mDlg, and mLgl also play important roles in epithelial cell polarity (Izumi et al., >>1998<<; Gao et al., 2002; Hirose et al., 2002; Lemmers et al., 2002; Roh et al., 2002, 2003; Suzuki et al., 2001, 2002; Hurd et al., 2003; Straight et al., 2004).
n3:mentions: n4:9763423

Subject Item: _:vb803994
rdf:type: n3:Context
rdf:value: The basolateral proteins Scrib, mDlg, and mLgl also play important roles in epithelial cell polarity (Izumi et al., 1998; Gao et al., >>2002<<; Hirose et al., 2002; Lemmers et al., 2002; Roh et al., 2002, 2003; Suzuki et al., 2001, 2002; Hurd et al., 2003; Straight et al., 2004).
n3:mentions: n4:11839275

Subject Item: _:vb803995
rdf:type: n3:Context
rdf:value: The basolateral proteins Scrib, mDlg, and mLgl also play important roles in epithelial cell polarity (Izumi et al., 1998; Gao et al., 2002; Hirose et al., >>2002<<; Lemmers et al., 2002; Roh et al., 2002, 2003; Suzuki et al., 2001, 2002; Hurd et al., 2003; Straight et al., 2004).
n3:mentions: n4:12045219

Subject Item: _:vb803996
rdf:type: n3:Context
rdf:value: The basolateral proteins Scrib, mDlg, and mLgl also play important roles in epithelial cell polarity (Izumi et al., 1998; Gao et al., 2002; Hirose et al., 2002; Lemmers et al., >>2002<<; Roh et al., 2002, 2003; Suzuki et al., 2001, 2002; Hurd et al., 2003; Straight et al., 2004).
n3:mentions: n4:11964389

Subject Item: _:vb803997
rdf:type: n3:Context
rdf:value: The basolateral proteins Scrib, mDlg, and mLgl also play important roles in epithelial cell polarity (Izumi et al., 1998; Gao et al., 2002; Hirose et al., 2002; Lemmers et al., 2002; Roh et al., >>2002<<, 2003; Suzuki et al., 2001, 2002; Hurd et al., 2003; Straight et al., 2004).
n3:mentions: n4:11927608

Subject Item: _:vb803998
rdf:type: n3:Context
rdf:value: The basolateral proteins Scrib, mDlg, and mLgl also play important roles in epithelial cell polarity (Izumi et al., 1998; Gao et al., 2002; Hirose et al., 2002; Lemmers et al., 2002; Roh et al., 2002, >>2003<<; Suzuki et al., 2001, 2002; Hurd et al., 2003; Straight et al., 2004).
n3:mentions: n4:12771187

Subject Item: _:vb803999
rdf:type: n3:Context
rdf:value: The basolateral proteins Scrib, mDlg, and mLgl also play important roles in epithelial cell polarity (Izumi et al., 1998; Gao et al., 2002; Hirose et al., 2002; Lemmers et al., 2002; Roh et al., 2002, 2003; Suzuki et al., >>2001<<, 2002; Hurd et al., 2003; Straight et al., 2004).
n3:mentions: n4:11257119

Subject Item: _:vb804000
rdf:type: n3:Context
rdf:value: The basolateral proteins Scrib, mDlg, and mLgl also play important roles in epithelial cell polarity (Izumi et al., 1998; Gao et al., 2002; Hirose et al., 2002; Lemmers et al., 2002; Roh et al., 2002, 2003; Suzuki et al., 2001, >>2002<<; Hurd et al., 2003; Straight et al., 2004).
n3:mentions: n4:12186943

Subject Item: _:vb804001
rdf:type: n3:Context
rdf:value: proteins Scrib, mDlg, and mLgl also play important roles in epithelial cell polarity (Izumi et al., 1998; Gao et al., 2002; Hirose et al., 2002; Lemmers et al., 2002; Roh et al., 2002, 2003; Suzuki et al., 2001, 2002; Hurd et al., >>2003<<; Straight et al., 2004).
n3:mentions: n4:12545177

Subject Item: _:vb804002
rdf:type: n3:Context
rdf:value: and mLgl also play important roles in epithelial cell polarity (Izumi et al., 1998; Gao et al., 2002; Hirose et al., 2002; Lemmers et al., 2002; Roh et al., 2002, 2003; Suzuki et al., 2001, 2002; Hurd et al., 2003; Straight et al., >>2004<<).
n3:mentions: n4:14718565

Subject Item: _:vb804003
rdf:type: n3:Context
rdf:value: In Drosophila, the Baz and Crb complexes not only colocalize in the apicolateral region of the cytocortex (Hong et al., >>2001<<; Bilder et al., 2003), but they interact physically by means of DPar-6 and Patj (Nam and Choi, 2003).
n3:mentions: n4:11740559

Subject Item: _:vb804004
rdf:type: n3:Context
rdf:value: In Drosophila, the Baz and Crb complexes not only colocalize in the apicolateral region of the cytocortex (Hong et al., 2001; Bilder et al., >>2003<<), but they interact physically by means of DPar-6 and Patj (Nam and Choi, 2003).
n3:mentions: n4:12510194

Subject Item: _:vb804005
rdf:type: n3:Context
rdf:value: In Drosophila, the Baz and Crb complexes not only colocalize in the apicolateral region of the cytocortex (Hong et al., 2001; Bilder et al., 2003), but they interact physically by means of DPar-6 and Patj (Nam and Choi, >>2003<<). Furthermore, absence of either complex similarly disrupts epithelial polarity (for review see Tepass et al., 2001), which suggests a functional relationship between them.
n3:mentions: n4:12900452

Subject Item: _:vb804006
rdf:type: n3:Context
rdf:value: Furthermore, absence of either complex similarly disrupts epithelial polarity (for review see Tepass et al., >>2001<<), which suggests a functional relationship between them.
n3:mentions: n4:11700298

Subject Item: _:vb804007
rdf:type: n2:Section
dc:title: materials and methods
n2:contains: _:vb804016 _:vb804017 _:vb804018 _:vb804019 _:vb804020 _:vb804021 _:vb804022 _:vb804008 _:vb804009 _:vb804010 _:vb804011 _:vb804012 _:vb804013 _:vb804014 _:vb804015

Subject Item: _:vb804008
rdf:type: n3:Context
rdf:value: kinase-dead DaPKC (UAS-DaPKC CAAXDN), membrane targeted kinase-dead Xenopus aPKCλ (UAS-XaPKCλCAAXDN) and wild-type and mutated membrane bound Crb-intra (UAS-Crbi) were generated by subcloning the corresponding cDNAs (Berra et al., >>1993<<; see Site directed mutagenesis) in the pUAST vector (Brand and Perrimon, 1993). The resulting pUAST-plasmids were used to transform w 1118 embryos (Ashburner, 1989) using 0.3 mg/ml of pUChsΔ2-3 as the source of transposase.
n3:mentions: n4:7688666

Subject Item: _:vb804009
rdf:type: n3:Context
rdf:value: aPKCλ (UAS-XaPKCλCAAXDN) and wild-type and mutated membrane bound Crb-intra (UAS-Crbi) were generated by subcloning the corresponding cDNAs (Berra et al., 1993; see Site directed mutagenesis) in the pUAST vector (Brand and Perrimon, >>1993<<). The resulting pUAST-plasmids were used to transform w 1118 embryos (Ashburner, 1989) using 0.3 mg/ml of pUChsΔ2-3 as the source of transposase.
n3:mentions: n4:8223268

Subject Item: _:vb804010
rdf:type: n3:Context
rdf:value: Mis-expression experiments were performed using the Gal4/UAS system (Brand and Perrimon, >>1993<<) and en-Gal4, Ubx-Gal4 (Calleja et al., 1996; a gift from M. Calleja, CBMSO, Madrid, Spain) and the maternal Gal4 line MatVP16V67-Gal4 (generated by D.
n3:mentions: n4:8223268

Subject Item: _:vb804011
rdf:type: n3:Context
rdf:value: Mis-expression experiments were performed using the Gal4/UAS system (Brand and Perrimon, 1993) and en-Gal4, Ubx-Gal4 (Calleja et al., >>1996<<; a gift from M. Calleja, CBMSO, Madrid, Spain) and the maternal Gal4 line MatVP16V67-Gal4 (generated by D.
n3:mentions: n4:8824191

Subject Item: _:vb804012
rdf:type: n3:Context
rdf:value: Embryos were fixed as in Tepass et al. (>>1990<<) and stained with rabbit anti-Patj and rat anti–Crb-intra (Bhat et al., 1999; a gift from H.
n3:mentions: n4:2344615

Subject Item: _:vb804013
rdf:type: n3:Context
rdf:value: Embryos were fixed as in Tepass et al. (1990) and stained with rabbit anti-Patj and rat anti–Crb-intra (Bhat et al., >>1999<<; a gift from H. Bellen, Baylor College of Medicine, Houston, TX), mouse Mab cq4 anti-Crb (DSHB), rabbit anti-Baz (a gift from A.
n3:mentions: n4:10102271

Subject Item: _:vb804014
rdf:type: n3:Context
rdf:value: , mouse Mab BP106 anti-Nrt (Hortsch et al., >>1990<<), rabbit anti-Scrib (a gift from C.
n3:mentions: n4:2100266

Subject Item: _:vb804015
rdf:type: n3:Context
rdf:value: Staining of en-Gal4/UAS-lacZ wings with X-gal (5-bromo-4-chloro-3-indolyl-β-d-galactopyranoside) was performed as described in Calleja et al. (>>1996<<).
n3:mentions: n4:8824191

Subject Item: _:vb804016
rdf:type: n3:Context
rdf:value: GST-fusion proteins were obtained from subclones in pGEX-3X (Amersham Biosciences) of full-length Patj (Bhat et al., >>1999<<), a gift from H. Bellen, and Crb wild-type or mutated intracellular domain (see Site directed mutagenesis) and CrbiΔERLI (Hong et al., 2001), a gift from Y.
n3:mentions: n4:10102271

Subject Item: _:vb804017
rdf:type: n3:Context
rdf:value: Bellen, and Crb wild-type or mutated intracellular domain (see Site directed mutagenesis) and CrbiΔERLI (Hong et al., >>2001<<), a gift from Y.
n3:mentions: n4:11740559

Subject Item: _:vb804018
rdf:type: n3:Context
rdf:value: 300 μg of Drosophila protein extract were incubated for 16 h at 4°C with 30 μg of GST or of the different GST-fusion proteins bound to glutathione beads as described in Sanz et al. (>>1999<<). Bound proteins were separated by SDS-PAGE and immunoblotted with anti-aPKCζ C20, anti-Baz (a gift from A. Wodarz), anti-DMoesin (from D. Kiehart, Duke University, Durham, NC) or anti-Patj antibodies. For in vitro binding assays,
n3:mentions: n4:10356400

Subject Item: _:vb804019
rdf:type: n3:Context
rdf:value: In vitro kinase assay were performed as in (Leitges et al., >>2001<<) using 30 ng of baculovirus-expressed recombinant human aPKCζ (Calbiochem) and 3 μg of the indicated GST-fusion proteins or of myelin basic protein.
n3:mentions: n4:11684013

Subject Item: _:vb804020
rdf:type: n3:Context
rdf:value: Generation of the UAS-Crb i construct was essentially as described previously (Wodarz et al., >>1995<<). crb cDNA (a gift from A. Wodarz) was used as a template to amplify the SP and TM domains using the following pairs of primers:
n3:mentions: n4:7606787

Subject Item: _:vb804021
rdf:type: n3:Context
rdf:value: pBluescript or pGEX-3X subclones containing the wild-type Crbi sequence (Wodarz et al., >>1995<<), were used as templates to obtain CrbiT6A with the following primers:
n3:mentions: n4:7606787

Subject Item: _:vb804022
rdf:type: n3:Context
rdf:value: pBluescript or pGEX-3X subclones containing the wild-type Crbi sequence (Wodarz et al., >>1995<<), were used as templates to obtain CrbiT6D with the following primers: 5′-CCAGGAACAAGCGAGCAGACAGGGGCACC-3′ and 5′-GGTGCCCCTGTCTGCTCGCTTGTTCCTGG-3′.
n3:mentions: n4:7606787

Subject Item: _:vb804023
rdf:type: n2:Section
dc:title: results
n2:contains: _:vb804024 _:vb804025 _:vb804026 _:vb804027 _:vb804028 _:vb804029 _:vb804030 _:vb804031 _:vb804032 _:vb804033 _:vb804034 _:vb804035 _:vb804036 _:vb804037 _:vb804038 _:vb804039

Subject Item: _:vb804024
rdf:type: n3:Context
rdf:value: In these cells, overexpression of a kinase-defective aPKC disrupts the assembly of the TJ (Suzuki et al., >>2001<<, 2002). We interfered with DaPKC signaling in vivo by overexpressing a form of DaPKC that was targeted to the cell membrane (by addition of the CAAX sequence), and that harbored a mutation (K293W) in the ATP binding site (DaPKC CAAXDN;
n3:mentions: n4:11257119

Subject Item: _:vb804025
rdf:type: n3:Context
rdf:value: In these cells, overexpression of a kinase-defective aPKC disrupts the assembly of the TJ (Suzuki et al., 2001, >>2002<<). We interfered with DaPKC signaling in vivo by overexpressing a form of DaPKC that was targeted to the cell membrane (by addition of the CAAX sequence), and that harbored a mutation (K293W) in the ATP binding site (DaPKC CAAXDN; see
n3:mentions: n4:12186943

Subject Item: _:vb804026
rdf:type: n3:Context
rdf:value: Similar modifications in Xenopus aPKCλ converted it into a kinase-inactive protein that acted as a dominant negative (DN; Berra et al., >>1993<<). We examined the subcellular distribution of apical (Fig. 1, A, D, and G, DaPKC, Crb, and Patj) and basolateral (Fig. 1 J, Scrib) markers in embryos overexpressing DaPKC CAAXDN using the Gal4/UAS system (Brand and Perrimon, 1993) with a
n3:mentions: n4:7688666

Subject Item: _:vb804027
rdf:type: n3:Context
rdf:value: 1 J, Scrib) markers in embryos overexpressing DaPKC CAAXDN using the Gal4/UAS system (Brand and Perrimon, >>1993<<) with a maternal Gal4 line (Fig.
n3:mentions: n4:8223268

Subject Item: _:vb804028
rdf:type: n3:Context
rdf:value: Conversely, accumulation of the basolateral marker Neurotactin (Nrt; Hortsch et al., >>1990<<), was significantly reduced (Fig.
n3:mentions: n4:2100266

Subject Item: _:vb804029
rdf:type: n3:Context
rdf:value: The colocalization of the Baz and Crb complexes (Hong et al., >>2001<<; Bilder et al., 2003) suggested that components of these two complexes might physically interact.
n3:mentions: n4:11740559

Subject Item: _:vb804030
rdf:type: n3:Context
rdf:value: The colocalization of the Baz and Crb complexes (Hong et al., 2001; Bilder et al., >>2003<<) suggested that components of these two complexes might physically interact. Indeed, in GST pull-down assays, the intracellular domain of Crumbs (Crbi) was able to precipitate DaPKC and Baz from embryonic extracts (Fig.
n3:mentions: n4:12510194

Subject Item: _:vb804031
rdf:type: n3:Context
rdf:value: for the interaction between the two apical complexes, we performed pull-down assays with CrbiΔERLI, a truncated form of Crbi devoid of the four COOH-terminal amino acids (ERLI) which constitute the Sdt binding domain (Bachmann et al., >>2001<<; Hong et al., 2001). As expected, CrbiΔERLI was unable to pull down Patj (Fig. 2 C).
n3:mentions: n4:11740560

Subject Item: _:vb804032
rdf:type: n3:Context
rdf:value: between the two apical complexes, we performed pull-down assays with CrbiΔERLI, a truncated form of Crbi devoid of the four COOH-terminal amino acids (ERLI) which constitute the Sdt binding domain (Bachmann et al., 2001; Hong et al., >>2001<<). As expected, CrbiΔERLI was unable to pull down Patj (Fig. 2 C). Interestingly, it was also unable to pull down DaPKC (Fig.
n3:mentions: n4:11740559

Subject Item: _:vb804033
rdf:type: n3:Context
rdf:value: Use of this driver enables direct comparison, in a single embryo, of the wild-type nonexpressing and the Crb-overexpressing domains (Fig. 4 A). As described previously (Wodarz et al., >>1995<<; Klebes and Knust, 2000), overexpression of membrane-tethered Crbi conferred partial apical character to the whole cell membrane, as shown by the distribution of DaPKC and Patj around the whole cell contour, coincident with the ectopic
n3:mentions: n4:7606787

Subject Item: _:vb804034
rdf:type: n3:Context
rdf:value: As described previously (Wodarz et al., 1995; Klebes and Knust, >>2000<<), overexpression of membrane-tethered Crbi conferred partial apical character to the whole cell membrane, as shown by the distribution of DaPKC and Patj around the whole cell contour, coincident with the ectopic distribution of Crb (Fig.
n3:mentions: n4:10662667

Subject Item: _:vb804035
rdf:type: n3:Context
rdf:value: of a nonphosphorylatable Crbi had the opposite effect than overexpression of wild-type Crbi and resembles the polarity phenotype of strong crb mutants, where Patj and DaPKC are lost from the plasma membrane (Bhat et al., >>1999<<; Klebes and Knust, 2000; Bilder et al., 2003). This suggested that the nonphosphorylatable Crbi acted as a DN.
n3:mentions: n4:10102271

Subject Item: _:vb804036
rdf:type: n3:Context
rdf:value: Crbi had the opposite effect than overexpression of wild-type Crbi and resembles the polarity phenotype of strong crb mutants, where Patj and DaPKC are lost from the plasma membrane (Bhat et al., 1999; Klebes and Knust, >>2000<<; Bilder et al., 2003). This suggested that the nonphosphorylatable Crbi acted as a DN.
n3:mentions: n4:10662667

Subject Item: _:vb804037
rdf:type: n3:Context
rdf:value: the opposite effect than overexpression of wild-type Crbi and resembles the polarity phenotype of strong crb mutants, where Patj and DaPKC are lost from the plasma membrane (Bhat et al., 1999; Klebes and Knust, 2000; Bilder et al., >>2003<<). This suggested that the nonphosphorylatable Crbi acted as a DN. Indeed, nonphosphorylatable Crbi was still able to pull down DaPKC, Patj, and DMoesin from embryonic extracts (Fig.
n3:mentions: n4:12510194

Subject Item: _:vb804038
rdf:type: n3:Context
rdf:value: Overexpression of Crbiwt caused severe tissue disorganization in the wing, an effect that has been attributed to apicalization of the wing disc cells (Fig. 4 J; Bilder et al., >>2003<<; Tanentzapf and Tepass, 2003).
n3:mentions: n4:12510194

Subject Item: _:vb804039
rdf:type: n3:Context
rdf:value: 4 J; Bilder et al., 2003; Tanentzapf and Tepass, >>2003<<). Although the overexpression of nonphosphorylatable CrbiT6AT9AS11AS13A generally lead to embryonic lethality, in a few cases, surviving flies were obtained and displayed only mild defects in the posterior crossvein (not depicted).
n3:mentions: n4:12510193

Subject Item: _:vb804040
rdf:type: n2:Section
dc:title: discussion
n2:contains: _:vb804044 _:vb804045 _:vb804046 _:vb804047 _:vb804041 _:vb804042 _:vb804043 _:vb804052 _:vb804053 _:vb804054 _:vb804055 _:vb804048 _:vb804049 _:vb804050 _:vb804051 _:vb804060 _:vb804061 _:vb804062 _:vb804063 _:vb804056 _:vb804057 _:vb804058 _:vb804059 _:vb804068 _:vb804069 _:vb804070 _:vb804071 _:vb804064 _:vb804065 _:vb804066 _:vb804067 _:vb804072 _:vb804073 _:vb804074

Subject Item: _:vb804041
rdf:type: n3:Context
rdf:value: The basolateral proteins Scrib, Lgl, and Dlg restrict the localization of the apical complexes, whereas the Crb complex appears to counteract the activity of these proteins (Bilder and Perrimon, >>2000<<; Bilder et al., 2000, 2003; Tanentzapf and Tepass, 2003).
n3:mentions: n4:10688207

Subject Item: _:vb804042
rdf:type: n3:Context
rdf:value: The basolateral proteins Scrib, Lgl, and Dlg restrict the localization of the apical complexes, whereas the Crb complex appears to counteract the activity of these proteins (Bilder and Perrimon, 2000; Bilder et al., >>2000<<, 2003; Tanentzapf and Tepass, 2003).
n3:mentions: n4:10884224

Subject Item: _:vb804043
rdf:type: n3:Context
rdf:value: The basolateral proteins Scrib, Lgl, and Dlg restrict the localization of the apical complexes, whereas the Crb complex appears to counteract the activity of these proteins (Bilder and Perrimon, 2000; Bilder et al., 2000, >>2003<<; Tanentzapf and Tepass, 2003).
n3:mentions: n4:12510194

Subject Item: _:vb804044
rdf:type: n3:Context
rdf:value: proteins Scrib, Lgl, and Dlg restrict the localization of the apical complexes, whereas the Crb complex appears to counteract the activity of these proteins (Bilder and Perrimon, 2000; Bilder et al., 2000, 2003; Tanentzapf and Tepass, >>2003<<). Recently, another basolateral protein, the Par-1 kinase has been involved in epithelial polarity.
n3:mentions: n4:12510193

Subject Item: _:vb804045
rdf:type: n3:Context
rdf:value: Par-1 inhibits formation of the Baz complex at the basolateral domain by blocking the oligomerization of Baz and its binding to DaPKC (Benton and Johnston, >>2003<<). In addition to these regulatory interactions, ours and previous data indicate a functional reciprocal interaction between the two apical complexes. Thus, DaPKC is required and instructive for membrane localization of Crb and Patj (this
n3:mentions: n4:14675534

Subject Item: _:vb804046
rdf:type: n3:Context
rdf:value: Conversely, the Crb complex is required to maintain the Baz complex at the apical membrane, as shown by the mislocalization of Baz and DaPKC in sdt or crb embryos (Bachmann et al., >>2001<<; Hong et al., 2001; Bilder et al., 2003).
n3:mentions: n4:11740560

Subject Item: _:vb804047
rdf:type: n3:Context
rdf:value: Conversely, the Crb complex is required to maintain the Baz complex at the apical membrane, as shown by the mislocalization of Baz and DaPKC in sdt or crb embryos (Bachmann et al., 2001; Hong et al., >>2001<<; Bilder et al., 2003).
n3:mentions: n4:11740559

Subject Item: _:vb804048
rdf:type: n3:Context
rdf:value: Conversely, the Crb complex is required to maintain the Baz complex at the apical membrane, as shown by the mislocalization of Baz and DaPKC in sdt or crb embryos (Bachmann et al., 2001; Hong et al., 2001; Bilder et al., >>2003<<). This functional interaction is supported by the synergism between sdt and baz mutations (Müller and Wieschaus, 1996). Thus, the similar mutant phenotypes associated with the absence of either of the apical complexes (Tepass et al.,
n3:mentions: n4:12510194

Subject Item: _:vb804049
rdf:type: n3:Context
rdf:value: This functional interaction is supported by the synergism between sdt and baz mutations (Müller and Wieschaus, >>1996<<). Thus, the similar mutant phenotypes associated with the absence of either of the apical complexes (Tepass et al., 2001) may then be accounted for by their functional relationship. Here, we show that physical interaction between the
n3:mentions: n4:8698811

Subject Item: _:vb804050
rdf:type: n3:Context
rdf:value: Thus, the similar mutant phenotypes associated with the absence of either of the apical complexes (Tepass et al., >>2001<<) may then be accounted for by their functional relationship.
n3:mentions: n4:11700298

Subject Item: _:vb804051
rdf:type: n3:Context
rdf:value: In mammalian epithelial cells in culture, overexpression of kinase-inactive aPKC disrupts the establishment of epithelial polarity (Suzuki et al., >>2001<<). Our results fully agree with these data. We have also found that overexpression in Drosophila embryos of Xenopus kinase-dead aPKCλ causes the same effects than overexpression of kinase-dead DaPKC (unpublished data).
n3:mentions: n4:11257119

Subject Item: _:vb804052
rdf:type: n3:Context
rdf:value: Thus, the zebra fish mutant Heart and soul encodes an aPKCλ mutated in a domain critical for the activation of its kinase function and this results in a defective ZA (Horne-Badovinac et al., >>2001<<). All these results show that the kinase activity of aPKC is necessary to establish epithelial polarity in different animal phila and poses the question as to the identification of the phosphorylation targets of DaPKC in epithelial cells.
n3:mentions: n4:11591316

Subject Item: _:vb804053
rdf:type: n3:Context
rdf:value: The identified targets of aPKC belong to two groups: basolateral proteins, negatively regulated by aPKC (Lgl, both in vertebrate and invertebrate cells [Betschinger et al., >>2003<<; Plant et al., 2003; Yamanaka et al., 2003] and mammalian Par-1 [Hurov et al., 2004]), and apical proteins, namely Par-3 (Hirose et al., 2002) and Crb (this work), which require such phosphorylation for their proper activity.
n3:mentions: n4:12629552

Subject Item: _:vb804054
rdf:type: n3:Context
rdf:value: The identified targets of aPKC belong to two groups: basolateral proteins, negatively regulated by aPKC (Lgl, both in vertebrate and invertebrate cells [Betschinger et al., 2003; Plant et al., >>2003<<; Yamanaka et al., 2003] and mammalian Par-1 [Hurov et al., 2004]), and apical proteins, namely Par-3 (Hirose et al., 2002) and Crb (this work), which require such phosphorylation for their proper activity.
n3:mentions: n4:12629547

Subject Item: _:vb804055
rdf:type: n3:Context
rdf:value: The identified targets of aPKC belong to two groups: basolateral proteins, negatively regulated by aPKC (Lgl, both in vertebrate and invertebrate cells [Betschinger et al., 2003; Plant et al., 2003; Yamanaka et al., >>2003<<] and mammalian Par-1 [Hurov et al., 2004]), and apical proteins, namely Par-3 (Hirose et al., 2002) and Crb (this work), which require such phosphorylation for their proper activity.
n3:mentions: n4:12725730

Subject Item: _:vb804056
rdf:type: n3:Context
rdf:value: regulated by aPKC (Lgl, both in vertebrate and invertebrate cells [Betschinger et al., 2003; Plant et al., 2003; Yamanaka et al., 2003] and mammalian Par-1 [Hurov et al., 2004]), and apical proteins, namely Par-3 (Hirose et al., >>2002<<) and Crb (this work), which require such phosphorylation for their proper activity.
n3:mentions: n4:12045219

Subject Item: _:vb804057
rdf:type: n3:Context
rdf:value: may be different in C. elegans, because the putatively phosphorylatable residues are absent from C. elegans Crb-1 and inactivation of crb-1 by dsRNAi did not disturb formation of the C. elegans apical junction (Bossinger et al., >>2001<<).
n3:mentions: n4:11161560

Subject Item: _:vb804058
rdf:type: n3:Context
rdf:value: for apicobasal polarity in Drosophila, as it is the case in cultured mammalian epithelial cells where phosphorylation of the mammalian homologue of Baz, ASIP/Par-3, by PKC-3 is indispensable for the formation of the TJ (Hirose et al., >>2002<<).
n3:mentions: n4:12045219

Subject Item: _:vb804059
rdf:type: n3:Context
rdf:value: Thus, in mammalian epithelial cells aPKC-dependent phosphorylation of Lgl and Par-1b prevents the association of these proteins with the plasma membrane (Yamanaka et al., >>2003<<; Hurov et al., 2004).
n3:mentions: n4:12725730

Subject Item: _:vb804060
rdf:type: n3:Context
rdf:value: Thus, in mammalian epithelial cells aPKC-dependent phosphorylation of Lgl and Par-1b prevents the association of these proteins with the plasma membrane (Yamanaka et al., 2003; Hurov et al., >>2004<<). In the apical side of the Drosophila neuroblasts, DaPKC counteracts the activity of Lgl releasing it from its association with the cell membrane (Betschinger et al., 2003). A similar antagonistic effect between DaPKC and Lgl and Dlg
n3:mentions: n4:15084291

Subject Item: _:vb804061
rdf:type: n3:Context
rdf:value: In the apical side of the Drosophila neuroblasts, DaPKC counteracts the activity of Lgl releasing it from its association with the cell membrane (Betschinger et al., >>2003<<). A similar antagonistic effect between DaPKC and Lgl and Dlg appears to take place in the imaginal discs (Rolls et al., 2003). In agreement with these observations, we have found that the kinase activity of DaPKC is required to exclude
n3:mentions: n4:12629552

Subject Item: _:vb804062
rdf:type: n3:Context
rdf:value: A similar antagonistic effect between DaPKC and Lgl and Dlg appears to take place in the imaginal discs (Rolls et al., >>2003<<). In agreement with these observations, we have found that the kinase activity of DaPKC is required to exclude Scrib from the apical region of the embryonic epithelial cells. This function of DaPKC would be independent of its role in Crb
n3:mentions: n4:14657233

Subject Item: _:vb804063
rdf:type: n3:Context
rdf:value: It has been proposed that the Baz, Crb, and Dlg complexes act sequentially to direct the maturation of epithelial cell polarity, the Baz complex being the first to be assembled and the most critical apical regulator (Bilder et al., >>2003<<). Our findings provide a mechanistic framework for the regulation of the Crb complex by the Baz complex.
n3:mentions: n4:12510194

Subject Item: _:vb804064
rdf:type: n3:Context
rdf:value: Thus, DPar-6 and Patj directly interact in vitro (Nam and Choi, >>2003<<). Now we find that DaPKC directly binds to Crb and Patj.
n3:mentions: n4:12900452

Subject Item: _:vb804065
rdf:type: n3:Context
rdf:value: Sdt is a likely candidate because it binds to this domain of Crb (Bachmann et al., >>2001<<; Hong et al., 2001; Roh et al., 2002) and its mammalian homologue Pals-1 binds Par-6 (Hurd et al., 2003).
n3:mentions: n4:11740560

Subject Item: _:vb804066
rdf:type: n3:Context
rdf:value: Sdt is a likely candidate because it binds to this domain of Crb (Bachmann et al., 2001; Hong et al., >>2001<<; Roh et al., 2002) and its mammalian homologue Pals-1 binds Par-6 (Hurd et al., 2003).
n3:mentions: n4:11740559

Subject Item: _:vb804067
rdf:type: n3:Context
rdf:value: Sdt is a likely candidate because it binds to this domain of Crb (Bachmann et al., 2001; Hong et al., 2001; Roh et al., >>2002<<) and its mammalian homologue Pals-1 binds Par-6 (Hurd et al., 2003).
n3:mentions: n4:11927608

Subject Item: _:vb804068
rdf:type: n3:Context
rdf:value: Sdt is a likely candidate because it binds to this domain of Crb (Bachmann et al., 2001; Hong et al., 2001; Roh et al., 2002) and its mammalian homologue Pals-1 binds Par-6 (Hurd et al., >>2003<<). Additionally, human Crb-3 and Par-6 interact (Lemmers et al., 2004), but it is not yet known whether this also occurs in Drosophila.
n3:mentions: n4:12545177

Subject Item: _:vb804069
rdf:type: n3:Context
rdf:value: Additionally, human Crb-3 and Par-6 interact (Lemmers et al., >>2004<<), but it is not yet known whether this also occurs in Drosophila.
n3:mentions: n4:14718572

Subject Item: _:vb804070
rdf:type: n3:Context
rdf:value: Thus, previous data suggested the existence of Crb-dependent and -independent mechanisms for the localization of Patj and Sdt (Tanentzapf et al., >>2000<<; Nam and Choi, 2003).
n3:mentions: n4:11076972

Subject Item: _:vb804071
rdf:type: n3:Context
rdf:value: Thus, previous data suggested the existence of Crb-dependent and -independent mechanisms for the localization of Patj and Sdt (Tanentzapf et al., 2000; Nam and Choi, >>2003<<). The interaction between components of the apical complexes, as stated by Nam and Choi (2003), would account for these results.
n3:mentions: n4:12900452

Subject Item: _:vb804072
rdf:type: n3:Context
rdf:value: The interaction between components of the apical complexes, as stated by Nam and Choi (>>2003<<), would account for these results.
n3:mentions: n4:12900452

Subject Item: _:vb804073
rdf:type: n3:Context
rdf:value: Additionally, there is a functional antagonism among the apical and the basolateral domain determining proteins (Bilder et al., >>2003<<, Tanentzapf and Tepass, 2003; this work).
n3:mentions: n4:12510194

Subject Item: _:vb804074
rdf:type: n3:Context
rdf:value: Additionally, there is a functional antagonism among the apical and the basolateral domain determining proteins (Bilder et al., 2003, Tanentzapf and Tepass, >>2003<<; this work).
n3:mentions: n4:12510193

Subject Item: _:vb293348750
rdf:type: n3:RelevantBibliographicResource
n3:RelevantScore: 15
n3:hasRelevantPaperId: n4:15177032

Subject Item: _:vb293348751
rdf:type: n3:RelevantBibliographicResource
n3:RelevantScore: 13
n3:hasRelevantPaperId: n4:7606787

Subject Item: _:vb293348752
rdf:type: n3:RelevantBibliographicResource
n3:RelevantScore: 12
n3:hasRelevantPaperId: n4:2344615

Subject Item: _:vb293348753
rdf:type: n3:RelevantBibliographicResource
n3:RelevantScore: 11
n3:hasRelevantPaperId: n4:12629552

Subject Item: _:vb293348754
rdf:type: n3:RelevantBibliographicResource
n3:RelevantScore: 11
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rdf:type: n3:RelevantBibliographicResource
n3:RelevantScore: 10
n3:hasRelevantPaperId: n4:12629547

Subject Item: _:vb293348756
rdf:type: n3:RelevantBibliographicResource
n3:RelevantScore: 10
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Subject Item: _:vb293348757
rdf:type: n3:RelevantBibliographicResource
n3:RelevantScore: 10
n3:hasRelevantPaperId: n4:12510193

Subject Item: _:vb293348758
rdf:type: n3:RelevantBibliographicResource
n3:RelevantScore: 10
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Subject Item: _:vb293348759
rdf:type: n3:RelevantBibliographicResource
n3:RelevantScore: 10
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Subject Item: _:vb293348760
rdf:type: n3:RelevantBibliographicResource
n3:RelevantScore: 10
n3:hasRelevantPaperId: n4:10662667

Subject Item: _:vb293348761
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n3:RelevantScore: 10
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n3:RelevantScore: 9
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rdf:type: n3:RelevantBibliographicResource
n3:RelevantScore: 9
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rdf:type: n3:RelevantBibliographicResource
n3:RelevantScore: 9
n3:hasRelevantPaperId: n4:19625503

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rdf:type: n3:RelevantBibliographicResource
n3:RelevantScore: 9
n3:hasRelevantPaperId: n4:12510194

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rdf:type: n3:RelevantBibliographicResource
n3:RelevantScore: 9
n3:hasRelevantPaperId: n4:11850625

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rdf:type: n3:RelevantBibliographicResource
n3:RelevantScore: 9
n3:hasRelevantPaperId: n4:16697075

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rdf:type: n3:RelevantBibliographicResource
n3:RelevantScore: 8
n3:hasRelevantPaperId: n4:14718572

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rdf:type: n3:RelevantBibliographicResource
n3:RelevantScore: 8
n3:hasRelevantPaperId: n4:10934475

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rdf:type: n3:RelevantBibliographicResource
n3:RelevantScore: 8
n3:hasRelevantPaperId: n4:16525119

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rdf:type: n3:RelevantBibliographicResource
n3:RelevantScore: 8
n3:hasRelevantPaperId: n4:16950127

Subject Item: _:vb293348772
rdf:type: n3:RelevantBibliographicResource
n3:RelevantScore: 8
n3:hasRelevantPaperId: n4:12545177

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rdf:type: n3:RelevantBibliographicResource
n3:RelevantScore: 8
n3:hasRelevantPaperId: n4:18976918

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rdf:type: n3:RelevantBibliographicResource
n3:RelevantScore: 8
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Subject Item: _:vb293348775
rdf:type: n3:RelevantBibliographicResource
n3:RelevantScore: 7
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Subject Item: _:vb293348776
rdf:type: n3:RelevantBibliographicResource
n3:RelevantScore: 7
n3:hasRelevantPaperId: n4:20110329

Subject Item: _:vb293348777
rdf:type: n3:RelevantBibliographicResource
n3:RelevantScore: 7
n3:hasRelevantPaperId: n4:26481050

Subject Item: _:vb293348778
rdf:type: n3:RelevantBibliographicResource
n3:RelevantScore: 7
n3:hasRelevantPaperId: n4:19789180

Subject Item: _:vb293348779
rdf:type: n3:RelevantBibliographicResource
n3:RelevantScore: 7
n3:hasRelevantPaperId: n4:24651541

Subject Item: _:vb293348780
rdf:type: n3:RelevantBibliographicResource
n3:RelevantScore: 7
n3:hasRelevantPaperId: n4:20819933

Subject Item: _:vb293348781
rdf:type: n3:RelevantBibliographicResource
n3:RelevantScore: 7
n3:hasRelevantPaperId: n4:10995441

Subject Item: _:vb293348782
rdf:type: n3:RelevantBibliographicResource
n3:RelevantScore: 7
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