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n2:pmcid: PMC0
bibo:doi: 10.1038%2Fncomms3976
n5:contains: _:vb27436060 _:vb27436075 _:vb27436016

Subject Item: _:vb27436016
rdf:type: n5:Section
dc:title: results
n5:contains: _:vb27436036 _:vb27436037 _:vb27436038 _:vb27436039 _:vb27436032 _:vb27436033 _:vb27436034 _:vb27436035 _:vb27436044 _:vb27436045 _:vb27436046 _:vb27436047 _:vb27436040 _:vb27436041 _:vb27436042 _:vb27436043 _:vb27436052 _:vb27436053 _:vb27436054 _:vb27436055 _:vb27436048 _:vb27436049 _:vb27436050 _:vb27436051 _:vb27436056 _:vb27436057 _:vb27436058 _:vb27436059 _:vb27436020 _:vb27436021 _:vb27436022 _:vb27436023 _:vb27436017 _:vb27436018 _:vb27436019 _:vb27436028 _:vb27436029 _:vb27436030 _:vb27436031 _:vb27436024 _:vb27436025 _:vb27436026 _:vb27436027

Subject Item: _:vb27436017
rdf:type: n2:Context
rdf:value: Hippo pathway perturbation can trigger tumorigenesis in mice, and mutations and altered expression of a subset of Hippo pathway genes have been observed in human cancers>>19<<20. To determine a potential role of ILK in the suppression of the Hippo pathway, we initially examined the phosphorylation status of YAP protein in different human tumour cell lines.
n2:mentions: n3:21138973

Subject Item: _:vb27436018
rdf:type: n2:Context
rdf:value: Hippo pathway perturbation can trigger tumorigenesis in mice, and mutations and altered expression of a subset of Hippo pathway genes have been observed in human cancers>>1920<<. To determine a potential role of ILK in the suppression of the Hippo pathway, we initially examined the phosphorylation status of YAP protein in different human tumour cell lines.
n2:mentions: n3:23467301

Subject Item: _:vb27436019
rdf:type: n2:Context
rdf:value: To examine the role of ILK in regulating the pathway in more detail, we treated PC3 and HCT116 human tumour cells with a highly specific inhibitor of ILK kinase activity>>16<<1821. This small molecule inhibitor, QLT0267, has previously been tested against 150 protein kinases and found to be highly selective at inhibiting ILK activity relative to other kinases21 with only one off-target kinase reported, the
n2:mentions: n3:22310280

Subject Item: _:vb27436020
rdf:type: n2:Context
rdf:value: To examine the role of ILK in regulating the pathway in more detail, we treated PC3 and HCT116 human tumour cells with a highly specific inhibitor of ILK kinase activity>>1618<<21. This small molecule inhibitor, QLT0267, has previously been tested against 150 protein kinases and found to be highly selective at inhibiting ILK activity relative to other kinases21 with only one off-target kinase reported, the
n2:mentions: n3:15630415

Subject Item: _:vb27436021
rdf:type: n2:Context
rdf:value: To examine the role of ILK in regulating the pathway in more detail, we treated PC3 and HCT116 human tumour cells with a highly specific inhibitor of ILK kinase activity>>161821<<. This small molecule inhibitor, QLT0267, has previously been tested against 150 protein kinases and found to be highly selective at inhibiting ILK activity relative to other kinases21 with only one off-target kinase reported, the FMS-like
n2:mentions: n3:16397254

Subject Item: _:vb27436022
rdf:type: n2:Context
rdf:value: This small molecule inhibitor, QLT0267, has previously been tested against 150 protein kinases and found to be highly selective at inhibiting ILK activity relative to other kinases>>21<< with only one off-target kinase reported, the FMS-like tyrosine kinase 3 (ref.
n2:mentions: n3:16397254

Subject Item: _:vb27436023
rdf:type: n2:Context
rdf:value: QLT0267, has previously been tested against 150 protein kinases and found to be highly selective at inhibiting ILK activity relative to other kinases21 with only one off-target kinase reported, the FMS-like tyrosine kinase 3 (ref. 22)>>22<<. As shown in Fig. 2a, treatment of these cell types, under standard growth conditions, with 10 μM QLT0267 resulted in a time-dependent stimulation of phosphorylation of MST1 (T183), LATS1 (T1079) and YAP (S127).
n2:mentions: n3:20193963

Subject Item: _:vb27436024
rdf:type: n2:Context
rdf:value: QLT0267 resulted in a time-dependent stimulation of phosphorylation of MST1 (T183), LATS1 (T1079) and YAP (S127). In addition, since phosphorylated YAP and TAZ have been demonstrated to be sequestered in the cytoplasm by 14.3.3 (ref. 8)>>8<<, we observed that in both cell lines, inhibition of ILK resulted in the sequestration of YAP to the cytoplasm with partial 14:
n2:mentions: n3:22659496

Subject Item: _:vb27436025
rdf:type: n2:Context
rdf:value: 2d), which is known to be activated by the YAP/TAZ transcriptional co-activators>>6<<. Since the YAP/TEAD transcription factor complex is known to activate genes involved in cell growth, we determined the effect of the ILK inhibitor on cell growth of PC3 cells. As shown in Fig. 2e, the growth of these cells was
n2:mentions: n3:20951342

Subject Item: _:vb27436026
rdf:type: n2:Context
rdf:value: The Hippo pathway has recently been reported to be regulated by G-protein-coupled receptor signalling through lysophosphatidic acid (LPA), as well as by epidermal growth factor (EGF)>>13<<23. In addition, TGF-β has been shown to activate YAP and YAP-mediated transcription24.
n2:mentions: n3:22863277

Subject Item: _:vb27436027
rdf:type: n2:Context
rdf:value: The Hippo pathway has recently been reported to be regulated by G-protein-coupled receptor signalling through lysophosphatidic acid (LPA), as well as by epidermal growth factor (EGF)>>1323<<. In addition, TGF-β has been shown to activate YAP and YAP-mediated transcription24.
n2:mentions: n3:23359693

Subject Item: _:vb27436028
rdf:type: n2:Context
rdf:value: In addition, TGF-β has been shown to activate YAP and YAP-mediated transcription>>24<<. Since ILK is an established effector of several growth factors, such as TGF-β, EGF, Wnt1 and Wnt3a161718, we wanted to determine whether ILK is required for the suppression of the Hippo pathway and YAP activation by these growth factors.
n2:mentions: n3:21145499

Subject Item: _:vb27436029
rdf:type: n2:Context
rdf:value: Since ILK is an established effector of several growth factors, such as TGF-β, EGF, Wnt1 and Wnt3a>>16<<1718, we wanted to determine whether ILK is required for the suppression of the Hippo pathway and YAP activation by these growth factors.
n2:mentions: n3:22310280

Subject Item: _:vb27436030
rdf:type: n2:Context
rdf:value: Since ILK is an established effector of several growth factors, such as TGF-β, EGF, Wnt1 and Wnt3a>>1617<<18, we wanted to determine whether ILK is required for the suppression of the Hippo pathway and YAP activation by these growth factors.
n2:mentions: n3:18799788

Subject Item: _:vb27436031
rdf:type: n2:Context
rdf:value: Since ILK is an established effector of several growth factors, such as TGF-β, EGF, Wnt1 and Wnt3a>>161718<<, we wanted to determine whether ILK is required for the suppression of the Hippo pathway and YAP activation by these growth factors.
n2:mentions: n3:15630415

Subject Item: _:vb27436032
rdf:type: n2:Context
rdf:value: In addition, nuclear localization of Smad 2/3 was induced in response to TGF-β1 signalling in MCF10A cells independent of ILK as shown previously>>16<< (Fig. 3b). However, TGF-β1-induced nuclear localization of YAP/TAZ was ILK dependent in MCF10A breast and BPH-1 prostate epithelial cells since co-incubation with the ILK inhibitor, QLT0267, or silencing its expression, resulted in the
n2:mentions: n3:22310280

Subject Item: _:vb27436033
rdf:type: n2:Context
rdf:value: The conserved Hippo pathway is stimulated in mammals by the FERM domain-containing tumour suppressor NF2 (neurofibromatosis type 2)/Merlin, resulting in the sequential activation of the MST1/2 and LATS1/2 kinases>>8<<. Because the inhibition of ILK in tumour cells significantly enhances the phosphorylation (and thus the activity) of MST1 and LATS1, the point at which ILK affects regulation of the pathway must be upstream of these kinases.
n2:mentions: n3:22659496

Subject Item: _:vb27436034
rdf:type: n2:Context
rdf:value: Since Merlin is required for MST1 activation>>25<<26, and Merlin activity is controlled by the phosphorylation status of Ser518 (refs 27, 28), we assessed whether ILK modulates Merlin activation.
n2:mentions: n3:22713867

Subject Item: _:vb27436035
rdf:type: n2:Context
rdf:value: Since Merlin is required for MST1 activation>>2526<<, and Merlin activity is controlled by the phosphorylation status of Ser518 (refs 27, 28), we assessed whether ILK modulates Merlin activation.
n2:mentions: n3:20491622

Subject Item: _:vb27436036
rdf:type: n2:Context
rdf:value: Since Merlin is required for MST1 activation2526, and Merlin activity is controlled by the phosphorylation status of Ser518 (refs >>27<<, 28), we assessed whether ILK modulates Merlin activation.
n2:mentions: n3:16885985

Subject Item: _:vb27436037
rdf:type: n2:Context
rdf:value: Since Merlin is required for MST1 activation2526, and Merlin activity is controlled by the phosphorylation status of Ser518 (refs 27, >>28<<), we assessed whether ILK modulates Merlin activation.
n2:mentions: n3:20178741

Subject Item: _:vb27436038
rdf:type: n2:Context
rdf:value: colon and breast cancer cells. However, inhibition of ILK activity resulted in dephosphorylation of Merlin Ser518 (Fig. 4a). Since Merlin is active when it is dephosphorylated at this site by the myosin phosphatase MYPT1-PP1 (ref. 27)>>27<< and MYPT1 phosphatase is also an established target of ILK2930, we wanted to determine whether ILK might modulate the Hippo pathway through MYPT1-mediated regulation of Merlin phosphorylation.
n2:mentions: n3:16885985

Subject Item: _:vb27436039
rdf:type: n2:Context
rdf:value: 27)27 and MYPT1 phosphatase is also an established target of ILK>>29<<30, we wanted to determine whether ILK might modulate the Hippo pathway through MYPT1-mediated regulation of Merlin phosphorylation.
n2:mentions: n3:12030846

Subject Item: _:vb27436040
rdf:type: n2:Context
rdf:value: 27)27 and MYPT1 phosphatase is also an established target of ILK>>2930<<, we wanted to determine whether ILK might modulate the Hippo pathway through MYPT1-mediated regulation of Merlin phosphorylation.
n2:mentions: n3:11931630

Subject Item: _:vb27436041
rdf:type: n2:Context
rdf:value: of ILK2930, we wanted to determine whether ILK might modulate the Hippo pathway through MYPT1-mediated regulation of Merlin phosphorylation. In PC3 cells, MYPT1 was constitutively phosphorylated at its inhibitory site, Thr696 (Fig. 4b)>>27<<2930. However, inhibition of ILK activity resulted in dephosphorylation of MYPT1 (Fig.
n2:mentions: n3:16885985

Subject Item: _:vb27436042
rdf:type: n2:Context
rdf:value: of ILK2930, we wanted to determine whether ILK might modulate the Hippo pathway through MYPT1-mediated regulation of Merlin phosphorylation. In PC3 cells, MYPT1 was constitutively phosphorylated at its inhibitory site, Thr696 (Fig. 4b)>>2729<<30. However, inhibition of ILK activity resulted in dephosphorylation of MYPT1 (Fig.
n2:mentions: n3:12030846

Subject Item: _:vb27436043
rdf:type: n2:Context
rdf:value: ILK2930, we wanted to determine whether ILK might modulate the Hippo pathway through MYPT1-mediated regulation of Merlin phosphorylation. In PC3 cells, MYPT1 was constitutively phosphorylated at its inhibitory site, Thr696 (Fig. 4b)>>272930<<. However, inhibition of ILK activity resulted in dephosphorylation of MYPT1 (Fig.
n2:mentions: n3:11931630

Subject Item: _:vb27436044
rdf:type: n2:Context
rdf:value: 4b), resulting in its activation as shown previously>>29<<30, and as determined by the observed dephosphorylation of its target Merlin (Fig.
n2:mentions: n3:12030846

Subject Item: _:vb27436045
rdf:type: n2:Context
rdf:value: 4b), resulting in its activation as shown previously>>2930<<, and as determined by the observed dephosphorylation of its target Merlin (Fig.
n2:mentions: n3:11931630

Subject Item: _:vb27436046
rdf:type: n2:Context
rdf:value: To confirm the specificity of ILK-dependent phosphorylation of MYPT1, especially since MYPT1 can also be phosphorylated at the inhibitory site by Rho kinase>>31<<, we treated PC3 cells with a Rho kinase-specific inhibitor, H1152.
n2:mentions: n3:20861082

Subject Item: _:vb27436047
rdf:type: n2:Context
rdf:value: confirm that ILK can directly phosphorylate MYPT1 on Thr696, we carried out an in vitro kinase assay utilizing highly purified active recombinant GST-ILK, which has been previously extensively characterized for its kinase characteristics>>32<<. As shown in Fig.
n2:mentions: n3:20827300

Subject Item: _:vb27436048
rdf:type: n2:Context
rdf:value: of the GST-ILK by SDS–polyacrylamide gel electrophoresis and staining of the gel with Coomassie blue showed the presence of a full-length protein with the expected molecular weight of ~78 kDa and purity of 94% as shown previously>>32<<. In addition, mass spectrometric analysis demonstrated the absence of other protein kinases in the GST-ILK preparation used for these studies32.
n2:mentions: n3:20827300

Subject Item: _:vb27436049
rdf:type: n2:Context
rdf:value: In addition, mass spectrometric analysis demonstrated the absence of other protein kinases in the GST-ILK preparation used for these studies>>32<<. This recombinant ILK directly phosphorylated MYPT1 on the inhibitory Thr696 residue in a dose and time-dependent manner (Fig. 4h), and this phosphorylation was inhibited by the ILK inhibitor, QLT0267 (Fig. 4i) but not by the Rho kinase
n2:mentions: n3:20827300

Subject Item: _:vb27436050
rdf:type: n2:Context
rdf:value: Finally, we examined the effect of ILK inhibition in U87 MG human malignant glioma cell line, in which Merlin expression has been shown to be dramatically reduced>>33<<, and also in Merlin-deficient Meso-33 mesothelioma cells34.
n2:mentions: n3:18632626

Subject Item: _:vb27436051
rdf:type: n2:Context
rdf:value: Finally, we examined the effect of ILK inhibition in U87 MG human malignant glioma cell line, in which Merlin expression has been shown to be dramatically reduced33, and also in Merlin-deficient Meso-33 mesothelioma cells>>34<<. As shown in Fig. 5b, no differences were observed in YAP/TAZ localization upon treatment of these cell lines with the ILK inhibitor, QLT0267. These data suggest that ILK regulates the Hippo pathway largely through MYPT1/Merlin axis,
n2:mentions: n3:21878678

Subject Item: _:vb27436052
rdf:type: n2:Context
rdf:value: the role of ILK in suppressing the Hippo pathway extended to tumours in vivo, we took advantage of two previously established transgenic breast cancer models in which the ILK gene was either deleted from ErbB2-induced breast tumours>>35<<, or was overexpressed together with Wnt1 in the mammary epithelium36.
n2:mentions: n3:20305688

Subject Item: _:vb27436053
rdf:type: n2:Context
rdf:value: in vivo, we took advantage of two previously established transgenic breast cancer models in which the ILK gene was either deleted from ErbB2-induced breast tumours35, or was overexpressed together with Wnt1 in the mammary epithelium>>36<<. In the former case deletion of ILK had a significant growth suppressive and anti-metastatic effect on ErbB2-driven mammary tumours35, whereas breast tumour growth in the double-transgenic Wnt1/ILK mice was significantly accelerated
n2:mentions: n3:20565980

Subject Item: _:vb27436054
rdf:type: n2:Context
rdf:value: In the former case deletion of ILK had a significant growth suppressive and anti-metastatic effect on ErbB2-driven mammary tumours>>35<<, whereas breast tumour growth in the double-transgenic Wnt1/ILK mice was significantly accelerated largely due to more rapid cell proliferation36.
n2:mentions: n3:20305688

Subject Item: _:vb27436055
rdf:type: n2:Context
rdf:value: a significant growth suppressive and anti-metastatic effect on ErbB2-driven mammary tumours35, whereas breast tumour growth in the double-transgenic Wnt1/ILK mice was significantly accelerated largely due to more rapid cell proliferation>>36<<. Here we now show that YAP/TAZ is highly expressed in ErbB2-driven mammary tumours (Fig.
n2:mentions: n3:20565980

Subject Item: _:vb27436056
rdf:type: n2:Context
rdf:value: We used MDA-MB-435 LCC6 cells, an established xenograft model for evaluating the efficacy of anti-cancer agents>>37<<, to first demonstrate the inhibition of TEAD transcriptional activity, induction of apoptosis and reduced cell growth in vitro following QLT0267 treatment (Fig.
n2:mentions: n3:21358264

Subject Item: _:vb27436057
rdf:type: n2:Context
rdf:value: ILK may promote cell growth and survival through activation of different signalling pathways such as PI3K/Akt>>17<<. To assess whether the induction of apoptosis and reduced cell growth observed following QLT0267 treatment in MDA-MB-435 cells was dependent on the inactivation of YAP/TAZ oncogenes, cells were transfected with an activated form of YAP
n2:mentions: n3:18799788

Subject Item: _:vb27436058
rdf:type: n2:Context
rdf:value: whether the induction of apoptosis and reduced cell growth observed following QLT0267 treatment in MDA-MB-435 cells was dependent on the inactivation of YAP/TAZ oncogenes, cells were transfected with an activated form of YAP (YAP S127A)>>12<<. Transfection of YAP S127A in MDA-MB-435 LCC6 cells prior to incubation with the ILK inhibitor QLT0267, resulted in a nearly complete rescue of apoptosis (Fig.
n2:mentions: n3:22891335

Subject Item: _:vb27436059
rdf:type: n2:Context
rdf:value: tumour cells within the tumours (Fig. 7g). A caveat of the effects of QLT0267 on tumour growth and YAP expression in mice could be through potential off-target effects due to the inhibition of other protein kinases as shown by Eke et al.>>38<< In conclusion, we have identified ILK as a critical player in the inactivation of the Hippo tumour suppressor pathway, via inactivation of the tumour suppressor Merlin.
n2:mentions: n3:19649326

Subject Item: _:vb27436060
rdf:type: n5:Section
dc:title: methods
n5:contains: _:vb27436061 _:vb27436062 _:vb27436063 _:vb27436068 _:vb27436069 _:vb27436070 _:vb27436071 _:vb27436064 _:vb27436065 _:vb27436066 _:vb27436067 _:vb27436072 _:vb27436073 _:vb27436074

Subject Item: _:vb27436061
rdf:type: n2:Context
rdf:value: Normal human epithelial MCF10A cells were cultured as previously described>>12<<16. NIC wild-type (WT) 9784 and 5257, were isolated from ErbB2-induced mammary tumours (NIC ILK wt/wt) and grown in DMEM with 5% fetal bovine serum, EGF (5 ng ml−1, Sigma-Aldrich), hydrocortisone (1 μg ml−1, Sigma-Aldrich), insulin (5 μg
n2:mentions: n3:22891335

Subject Item: _:vb27436062
rdf:type: n2:Context
rdf:value: Normal human epithelial MCF10A cells were cultured as previously described>>1216<<. NIC wild-type (WT) 9784 and 5257, were isolated from ErbB2-induced mammary tumours (NIC ILK wt/wt) and grown in DMEM with 5% fetal bovine serum, EGF (5 ng ml−1, Sigma-Aldrich), hydrocortisone (1 μg ml−1, Sigma-Aldrich), insulin (5 μg
n2:mentions: n3:22310280

Subject Item: _:vb27436063
rdf:type: n2:Context
rdf:value: mammary tumours (NIC ILK wt/wt) and grown in DMEM with 5% fetal bovine serum, EGF (5 ng ml−1, Sigma-Aldrich), hydrocortisone (1 μg ml−1, Sigma-Aldrich), insulin (5 μg ml−1, Sigma-Aldrich) and bovine pituitary extract (Lonza)>>35<<. Meso-33 cells were a gift from Dr Filippo G. Giancotti (Memorial Sloan-Kettering Cancer Center (MSKCC), New York, NY, USA).
n2:mentions: n3:20305688

Subject Item: _:vb27436064
rdf:type: n2:Context
rdf:value: For siRNA (small interference) transfection, cells were transfected using SilentFect (Bio-Rad Laboratories) as previously shown>>16<<. ILK was targeted, as previously validated1654, using ILK-A, DNA target sequence:
n2:mentions: n3:22310280

Subject Item: _:vb27436065
rdf:type: n2:Context
rdf:value: ILK was targeted, as previously validated>>16<<54, using ILK-A, DNA target sequence:
n2:mentions: n3:22310280

Subject Item: _:vb27436066
rdf:type: n2:Context
rdf:value: ILK was targeted, as previously validated>>1654<<, using ILK-A, DNA target sequence:
n2:mentions: n3:20838383

Subject Item: _:vb27436067
rdf:type: n2:Context
rdf:value: Cells were harvested and RIPA lysed as described previously>>16<<. For immunoprecipitation experiments, cells were pelleted and resuspended in 400 μl of 10 mM HEPES-potassium hydroxide (pH 7.9), 1.5 mM magnesium chloride, 10 mM potassium chloride, 0.5 mM dithiothreitol and 0.2 mM phenylmethylsulphonyl
n2:mentions: n3:22310280

Subject Item: _:vb27436068
rdf:type: n2:Context
rdf:value: Tubes were incubated for 20 min on ice and then centrifuged to clear the cellular debris>>53<<. Protein concentrations were determined using the BCA assay (Pierce Biotechnology). Immunoprecipitation of 1 mg protein was carried in the cytoplasmic cell fraction with 5 μg anti-TAZ antibody (cat. no. 560235, BD Bioscience) or the
n2:mentions: n3:16799642

Subject Item: _:vb27436069
rdf:type: n2:Context
rdf:value: Immunoblotting was carried out as previously described>>16<<. Proteins were separated on NuPAGE 4–12% gradient gels (Invitrogen). Samples were incubated overnight at 4 °C with appropriate primary antibodies at a dilution of 1:
n2:mentions: n3:22310280

Subject Item: _:vb27436070
rdf:type: n2:Context
rdf:value: Non-radioactive ILK kinase activity assays were performed as previously described>>32<<. Briefly, 100 ng of highly purified GST-ILK (SignalChem Lifesciences Corporation, Richmond, BC, Canada), 500 ng of the substrate MYPT1 (EMD Millipore, Billerica, MA) and 500 μM cold ATP were incubated in kinase buffer (New England
n2:mentions: n3:20827300

Subject Item: _:vb27436071
rdf:type: n2:Context
rdf:value: ErbB2-induced mammary tumours (NIC ILK wt/wt) or mammary gland targeted deletion of ILK tumours (NIC ILK f/f) have been generated and characterized>>35<<. To mitigate the impact of genetic background variability, transgenic mice were derived from the inbred FVB/N strain.
n2:mentions: n3:20305688

Subject Item: _:vb27436072
rdf:type: n2:Context
rdf:value: The generation of mammary-specific double-transgenic MMTV-Wnt/ILK mice has been described by us>>36<<. Briefly, MMTV-Wnt1 and MMTV-ILK mice were backcrossed to the FVB strain. MMTV-Wnt1 males were then bred with MMTV-ILK female to generate the double-transgenic MMTV-Wnt/ILK mice.
n2:mentions: n3:20565980

Subject Item: _:vb27436073
rdf:type: n2:Context
rdf:value: Immunohistochemistry analysis was performed as previously described>>35<<55. Briefly, antigen retrieval was accomplished in citrate buffer by using a microwave and peroxidase activity was blocked with 3% peroxide hydrogen.
n2:mentions: n3:20305688

Subject Item: _:vb27436074
rdf:type: n2:Context
rdf:value: Immunohistochemistry analysis was performed as previously described>>3555<<. Briefly, antigen retrieval was accomplished in citrate buffer by using a microwave and peroxidase activity was blocked with 3% peroxide hydrogen.
n2:mentions: n3:22971619

Subject Item: _:vb27436075
rdf:type: n5:Section
dc:title: discussion
n5:contains: _:vb27436104 _:vb27436105 _:vb27436106 _:vb27436107 _:vb27436108 _:vb27436109 _:vb27436110 _:vb27436111 _:vb27436096 _:vb27436097 _:vb27436098 _:vb27436099 _:vb27436100 _:vb27436101 _:vb27436102 _:vb27436103 _:vb27436112 _:vb27436113 _:vb27436114 _:vb27436115 _:vb27436076 _:vb27436077 _:vb27436078 _:vb27436079 _:vb27436088 _:vb27436089 _:vb27436090 _:vb27436091 _:vb27436092 _:vb27436093 _:vb27436094 _:vb27436095 _:vb27436080 _:vb27436081 _:vb27436082 _:vb27436083 _:vb27436084 _:vb27436085 _:vb27436086 _:vb27436087

Subject Item: _:vb27436076
rdf:type: n2:Context
rdf:value: The communication between cells and their microenvironment can influence activation or inactivation of intracellular signalling pathways and the survival of tumour cells depends on their ability to adapt to their environment>>3<<46. Integration of signalling pathways for the adequate balance of cell proliferation and apoptosis is an essential function of multicellular organism under physiological conditions and deregulation of these functions leads to human
n2:mentions: n3:15652746

Subject Item: _:vb27436077
rdf:type: n2:Context
rdf:value: The communication between cells and their microenvironment can influence activation or inactivation of intracellular signalling pathways and the survival of tumour cells depends on their ability to adapt to their environment>>34<<6. Integration of signalling pathways for the adequate balance of cell proliferation and apoptosis is an essential function of multicellular organism under physiological conditions and deregulation of these functions leads to human
n2:mentions: n3:18984162

Subject Item: _:vb27436078
rdf:type: n2:Context
rdf:value: The communication between cells and their microenvironment can influence activation or inactivation of intracellular signalling pathways and the survival of tumour cells depends on their ability to adapt to their environment>>346<<. Integration of signalling pathways for the adequate balance of cell proliferation and apoptosis is an essential function of multicellular organism under physiological conditions and deregulation of these functions leads to human diseases
n2:mentions: n3:20951342

Subject Item: _:vb27436079
rdf:type: n2:Context
rdf:value: Although the transcription co-activators, YAP and TAZ, are well-established Hippo signalling downstream oncogenes in several cell types and promote metastasis>>6<<122539, many efforts are now directed towards identifying the upstream regulators of the pathway.
n2:mentions: n3:20951342

Subject Item: _:vb27436080
rdf:type: n2:Context
rdf:value: Although the transcription co-activators, YAP and TAZ, are well-established Hippo signalling downstream oncogenes in several cell types and promote metastasis>>612<<2539, many efforts are now directed towards identifying the upstream regulators of the pathway.
n2:mentions: n3:22891335

Subject Item: _:vb27436081
rdf:type: n2:Context
rdf:value: Although the transcription co-activators, YAP and TAZ, are well-established Hippo signalling downstream oncogenes in several cell types and promote metastasis>>61225<<39, many efforts are now directed towards identifying the upstream regulators of the pathway.
n2:mentions: n3:22713867

Subject Item: _:vb27436082
rdf:type: n2:Context
rdf:value: Although the transcription co-activators, YAP and TAZ, are well-established Hippo signalling downstream oncogenes in several cell types and promote metastasis>>6122539<<, many efforts are now directed towards identifying the upstream regulators of the pathway.
n2:mentions: n3:16894141

Subject Item: _:vb27436083
rdf:type: n2:Context
rdf:value: Other kinases such as homeodomain-interacting protein kinase (HIPK2) have been recently identified to modulate YAP>>40<<. However, in contrast to ILK, which we have demonstrated is upstream of LATS phosphorylation and activation, regulation of YAP by HIPK2 occurs in parallel to LATS activation40.
n2:mentions: n3:22840515

Subject Item: _:vb27436084
rdf:type: n2:Context
rdf:value: However, in contrast to ILK, which we have demonstrated is upstream of LATS phosphorylation and activation, regulation of YAP by HIPK2 occurs in parallel to LATS activation>>40<<.
n2:mentions: n3:22840515

Subject Item: _:vb27436085
rdf:type: n2:Context
rdf:value: In the context of normal hepatic biology and control of organ size, it has been reported that targeted knockout of ILK in the liver results in increased expression of total YAP during liver regeneration>>41<<. Overall lower phosphorylation of YAP in the knockout animals was also reported in this study, although results were not quantified and other components of the Hippo pathway were not interrogated41.
n2:mentions: n3:19575460

Subject Item: _:vb27436086
rdf:type: n2:Context
rdf:value: Overall lower phosphorylation of YAP in the knockout animals was also reported in this study, although results were not quantified and other components of the Hippo pathway were not interrogated>>41<<. Importantly, we have demonstrated in this study that ILK is a critical upstream regulator of Hippo signalling in cancer cells and that inhibition of ILK leads to changes in the phosphorylation status of several of the core components of
n2:mentions: n3:19575460

Subject Item: _:vb27436087
rdf:type: n2:Context
rdf:value: The differences between the data described here and those reported by Apte et al.>>41<< may be due, in part, to the contrasting roles of ILK signalling in normal cells and cancer cells, as has been established previously for the survival of cancer cells, which are critically dependent on ILK signalling, compared with
n2:mentions: n3:19575460

Subject Item: _:vb27436088
rdf:type: n2:Context
rdf:value: roles of ILK signalling in normal cells and cancer cells, as has been established previously for the survival of cancer cells, which are critically dependent on ILK signalling, compared with ILK-independent survival by normal cells>>21<<.
n2:mentions: n3:16397254

Subject Item: _:vb27436089
rdf:type: n2:Context
rdf:value: Merlin is a multifunctional protein and recent studies suggest that Merlin is also an upstream component of the mammalian Hippo pathway>>26<<424344. Our results demonstrate that in the tumour cell types in which the Hippo pathway is inactivated, Merlin is phosphorylated on Ser518. Inhibiting or silencing ILK resulted in dephosphorylation of Merlin at this site, and since
n2:mentions: n3:20491622

Subject Item: _:vb27436090
rdf:type: n2:Context
rdf:value: Merlin is a multifunctional protein and recent studies suggest that Merlin is also an upstream component of the mammalian Hippo pathway>>2642<<4344. Our results demonstrate that in the tumour cell types in which the Hippo pathway is inactivated, Merlin is phosphorylated on Ser518. Inhibiting or silencing ILK resulted in dephosphorylation of Merlin at this site, and since
n2:mentions: n3:18725387

Subject Item: _:vb27436091
rdf:type: n2:Context
rdf:value: Merlin is a multifunctional protein and recent studies suggest that Merlin is also an upstream component of the mammalian Hippo pathway>>264243<<44. Our results demonstrate that in the tumour cell types in which the Hippo pathway is inactivated, Merlin is phosphorylated on Ser518. Inhibiting or silencing ILK resulted in dephosphorylation of Merlin at this site, and since activation
n2:mentions: n3:22618028

Subject Item: _:vb27436092
rdf:type: n2:Context
rdf:value: Merlin is a multifunctional protein and recent studies suggest that Merlin is also an upstream component of the mammalian Hippo pathway>>26424344<<. Our results demonstrate that in the tumour cell types in which the Hippo pathway is inactivated, Merlin is phosphorylated on Ser518. Inhibiting or silencing ILK resulted in dephosphorylation of Merlin at this site, and since activation
n2:mentions: n3:23431053

Subject Item: _:vb27436093
rdf:type: n2:Context
rdf:value: Inhibiting or silencing ILK resulted in dephosphorylation of Merlin at this site, and since activation of Merlin occurs upon its dephosphorylation>>27<<, ILK most likely regulates Merlin phosphorylation via phospho-inhibition of a phosphatase.
n2:mentions: n3:16885985

Subject Item: _:vb27436094
rdf:type: n2:Context
rdf:value: It has been shown that Merlin is the decisive substrate of MYPT1-PP1 in tumour suppression>>27<< and here we have demonstrated that ILK specifically phosphorylates MYPT1 to inhibit its activity.
n2:mentions: n3:16885985

Subject Item: _:vb27436095
rdf:type: n2:Context
rdf:value: The GST-ILK preparation used to perform the kinase assay experiments reported in this study has been extensively characterized>>32<<. In fact, mass spectrometric analysis of the highly purified preparation did not detect any other protein kinases, besides ILK32, demonstrating that ILK alone is responsible for MYPT1 phosphorylation in this assay. Furthermore, inhibition
n2:mentions: n3:20827300

Subject Item: _:vb27436096
rdf:type: n2:Context
rdf:value: In fact, mass spectrometric analysis of the highly purified preparation did not detect any other protein kinases, besides ILK>>32<<, demonstrating that ILK alone is responsible for MYPT1 phosphorylation in this assay.
n2:mentions: n3:20827300

Subject Item: _:vb27436097
rdf:type: n2:Context
rdf:value: is directly phosphorylated by purified ILK in vitro and that this phosphorylation is inhibited by QLT0267, but not by a Rho kinase inhibitor, constitute further convincing evidence that ILK is an active, physiologically relevant kinase>>45<<.
n2:mentions: n3:21602880

Subject Item: _:vb27436098
rdf:type: n2:Context
rdf:value: Recently, numerous upstream components involved in the Hippo pathway have been identified, such as cell polarity, mechanotransduction and G-protein-coupled receptor signalling>>44<<46, and Hippo signalling has been shown to be regulated by cell detachment and by growth factors1314.
n2:mentions: n3:23431053

Subject Item: _:vb27436099
rdf:type: n2:Context
rdf:value: Recently, numerous upstream components involved in the Hippo pathway have been identified, such as cell polarity, mechanotransduction and G-protein-coupled receptor signalling>>4446<<, and Hippo signalling has been shown to be regulated by cell detachment and by growth factors1314.
n2:mentions: n3:21654799

Subject Item: _:vb27436100
rdf:type: n2:Context
rdf:value: involved in the Hippo pathway have been identified, such as cell polarity, mechanotransduction and G-protein-coupled receptor signalling4446, and Hippo signalling has been shown to be regulated by cell detachment and by growth factors>>13<<14. We found that the suppression of the Hippo pathway by the tumour microenvironmental factors TGF-β, EGF and LPA is ILK dependent.
n2:mentions: n3:22863277

Subject Item: _:vb27436101
rdf:type: n2:Context
rdf:value: involved in the Hippo pathway have been identified, such as cell polarity, mechanotransduction and G-protein-coupled receptor signalling4446, and Hippo signalling has been shown to be regulated by cell detachment and by growth factors>>1314<<. We found that the suppression of the Hippo pathway by the tumour microenvironmental factors TGF-β, EGF and LPA is ILK dependent.
n2:mentions: n3:22215811

Subject Item: _:vb27436102
rdf:type: n2:Context
rdf:value: Both ILK and YAP/TAZ protein levels are frequently elevated in many types of human cancers>>17<<25474849, although whether these elevated levels interact functionally has not been determined.
n2:mentions: n3:18799788

Subject Item: _:vb27436103
rdf:type: n2:Context
rdf:value: Both ILK and YAP/TAZ protein levels are frequently elevated in many types of human cancers>>1725<<474849, although whether these elevated levels interact functionally has not been determined.
n2:mentions: n3:22713867

Subject Item: _:vb27436104
rdf:type: n2:Context
rdf:value: Both ILK and YAP/TAZ protein levels are frequently elevated in many types of human cancers>>172547<<4849, although whether these elevated levels interact functionally has not been determined.
n2:mentions: n3:18413727

Subject Item: _:vb27436105
rdf:type: n2:Context
rdf:value: Both ILK and YAP/TAZ protein levels are frequently elevated in many types of human cancers>>17254748<<49, although whether these elevated levels interact functionally has not been determined.
n2:mentions: n3:18703216

Subject Item: _:vb27436106
rdf:type: n2:Context
rdf:value: Both ILK and YAP/TAZ protein levels are frequently elevated in many types of human cancers>>1725474849<<, although whether these elevated levels interact functionally has not been determined.
n2:mentions: n3:17974916

Subject Item: _:vb27436107
rdf:type: n2:Context
rdf:value: First, in ErbB2-induced mammary tumours, where YAP/TAZ are highly expressed and active, deletion of ILK had a significant suppression of YAP/TAZ expression, correlating with a marked suppression of tumour growth and metastasis>>35<<. The overall decrease in YAP protein expression in the ILK knockout tumours is somewhat different from what we observed with ILK knockdown or inhibition of activity in cultured cells where the overall levels of YAP/TAZ were not
n2:mentions: n3:20305688

Subject Item: _:vb27436108
rdf:type: n2:Context
rdf:value: The overall decrease in the YAP/TAZ protein levels in these tumours in vivo is not surprising however, since YAP/TAZ phosphorylation also leads to its degradation>>49<<, and long-term sequestration in the cytoplasm would also lead to eventual degradation.
n2:mentions: n3:17974916

Subject Item: _:vb27436109
rdf:type: n2:Context
rdf:value: Recently, coordinated phosphorylation of YAP by LATS and CK1 on Ser381 has been shown to regulate the stability of YAP>>50<<, and this could account for the loss of YAP expression in the ILK knockout tumours.
n2:mentions: n3:20048001

Subject Item: _:vb27436110
rdf:type: n2:Context
rdf:value: Second, we have shown the converse situation where tumours that overexpress ILK in the background of Wnt activation leads to accelerated tumour growth>>36<< and have increased and strong nuclear expression of YAP/TAZ proteins. Wnt signalling is known to activate the expression of YAP/TAZ51, and β-catenin-driven cancers require YAP transcriptional complex for tumorigenesis52.
n2:mentions: n3:20565980

Subject Item: _:vb27436111
rdf:type: n2:Context
rdf:value: Wnt signalling is known to activate the expression of YAP/TAZ>>51<<, and β-catenin-driven cancers require YAP transcriptional complex for tumorigenesis52.
n2:mentions: n3:22234184

Subject Item: _:vb27436112
rdf:type: n2:Context
rdf:value: Wnt signalling is known to activate the expression of YAP/TAZ51, and β-catenin-driven cancers require YAP transcriptional complex for tumorigenesis>>52<<. Since ILK also activates the downstream components of the Wnt signalling pathway, especially β-catenin stabilization53, and it cooperates with Wnt1 to accelerate breast tumour growth36, it is not surprising to observe significant
n2:mentions: n3:23245941

Subject Item: _:vb27436113
rdf:type: n2:Context
rdf:value: Since ILK also activates the downstream components of the Wnt signalling pathway, especially β-catenin stabilization>>53<<, and it cooperates with Wnt1 to accelerate breast tumour growth36, it is not surprising to observe significant stimulation of nuclear YAP expression in tumours from the double-transgenic ILK/Wnt1 mice.
n2:mentions: n3:16799642

Subject Item: _:vb27436114
rdf:type: n2:Context
rdf:value: Since ILK also activates the downstream components of the Wnt signalling pathway, especially β-catenin stabilization53, and it cooperates with Wnt1 to accelerate breast tumour growth>>36<<, it is not surprising to observe significant stimulation of nuclear YAP expression in tumours from the double-transgenic ILK/Wnt1 mice.
n2:mentions: n3:20565980

Subject Item: _:vb27436115
rdf:type: n2:Context
rdf:value: Third, treatment with QLT0267 in MDA-MB-435 LCC6 established xenograft model for evaluating the efficacy of anti-cancer agents>>37<<, resulted in significant tumour growth suppression with inhibition of expression of nuclear YAP/TAZ in the tumour cells within the tumours.
n2:mentions: n3:21358264

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