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10.1371%2Fjournal.pone.0024288
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introduction
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pathway has been delineated as a tumor suppressor pathway, which has been implicated in the diverse biological processes including cell proliferation, apoptosis, organ size control, and cancer development in both Drosophila and mammals [>>1<<], [2], [3].
n2:mentions
n3:17889654
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has been delineated as a tumor suppressor pathway, which has been implicated in the diverse biological processes including cell proliferation, apoptosis, organ size control, and cancer development in both Drosophila and mammals [1], [>>2<<], [3]. MST1 and MST2 (mammalian STE-20 like kinase 1 and 2) are key components of the Hippo/MST1 tumor suppressor pathway [4], [5], and we have reported that MST1 mediates oxidative stress-induced neuronal cell death through
n2:mentions
n3:20439427
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_:vb12486176
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been delineated as a tumor suppressor pathway, which has been implicated in the diverse biological processes including cell proliferation, apoptosis, organ size control, and cancer development in both Drosophila and mammals [1], [2], [>>3<<]. MST1 and MST2 (mammalian STE-20 like kinase 1 and 2) are key components of the Hippo/MST1 tumor suppressor pathway [4], [5], and we have reported that MST1 mediates oxidative stress-induced neuronal cell death through phosphorylating
n2:mentions
n3:12535517
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_:vb12486177
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MST1 and MST2 (mammalian STE-20 like kinase 1 and 2) are key components of the Hippo/MST1 tumor suppressor pathway [>>4<<], [5], and we have reported that MST1 mediates oxidative stress-induced neuronal cell death through phosphorylating FOXO3a at serine 207 [6].
n2:mentions
n3:20619814
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_:vb12486178
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MST1 and MST2 (mammalian STE-20 like kinase 1 and 2) are key components of the Hippo/MST1 tumor suppressor pathway [4], [>>5<<], and we have reported that MST1 mediates oxidative stress-induced neuronal cell death through phosphorylating FOXO3a at serine 207 [6].
n2:mentions
n3:16096061
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_:vb12486179
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STE-20 like kinase 1 and 2) are key components of the Hippo/MST1 tumor suppressor pathway [4], [5], and we have reported that MST1 mediates oxidative stress-induced neuronal cell death through phosphorylating FOXO3a at serine 207 [>>6<<]. Others and we also showed that PI3K/Akt and JNK regulate MST1 activation through protein interaction and phosphorylation during stress-induced cell death [7], [8], [9].
n2:mentions
n3:16751106
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Others and we also showed that PI3K/Akt and JNK regulate MST1 activation through protein interaction and phosphorylation during stress-induced cell death [>>7<<], [8], [9].
n2:mentions
n3:19940129
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Others and we also showed that PI3K/Akt and JNK regulate MST1 activation through protein interaction and phosphorylation during stress-induced cell death [7], [>>8<<], [9].
n2:mentions
n3:17932490
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Others and we also showed that PI3K/Akt and JNK regulate MST1 activation through protein interaction and phosphorylation during stress-induced cell death [7], [8], [>>9<<].
n2:mentions
n3:11442632
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YAP2 was initially identified as a Src/Yes kinase associated protein [>>10<<]. Structurally, YAP2 contains one TEAD (TEF domain) binding domain in the N-terminus followed by two WW domains and PDZ binding motif in the C-tail [11], [12].
n2:mentions
n3:2067844
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Structurally, YAP2 contains one TEAD (TEF domain) binding domain in the N-terminus followed by two WW domains and PDZ binding motif in the C-tail [>>11<<], [12]. Multiple lines of evidences have shown that YAP2 functions as a transcriptional co-activator and downstream target of the Hippo/MST pathway in the biological processes of cell size control, proliferation and cell death[1], [2],
n2:mentions
n3:10228168
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Structurally, YAP2 contains one TEAD (TEF domain) binding domain in the N-terminus followed by two WW domains and PDZ binding motif in the C-tail [11], [>>12<<]. Multiple lines of evidences have shown that YAP2 functions as a transcriptional co-activator and downstream target of the Hippo/MST pathway in the biological processes of cell size control, proliferation and cell death[1], [2], [3], [13].
n2:mentions
n3:11358867
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_:vb12486186
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Multiple lines of evidences have shown that YAP2 functions as a transcriptional co-activator and downstream target of the Hippo/MST pathway in the biological processes of cell size control, proliferation and cell death[>>1<<], [2], [3], [13].
n2:mentions
n3:17889654
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Multiple lines of evidences have shown that YAP2 functions as a transcriptional co-activator and downstream target of the Hippo/MST pathway in the biological processes of cell size control, proliferation and cell death[1], [>>2<<], [3], [13].
n2:mentions
n3:20439427
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Multiple lines of evidences have shown that YAP2 functions as a transcriptional co-activator and downstream target of the Hippo/MST pathway in the biological processes of cell size control, proliferation and cell death[1], [2], [>>3<<], [13]. It has recently been shown that Mst1/2 ablation leads to hepatocellular carcinomas and the inhibition of YAP2 by MST kinases are an important mechanism in tumor suppression, especially in the progression of HCC (hepatocellular
n2:mentions
n3:12535517
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_:vb12486189
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Multiple lines of evidences have shown that YAP2 functions as a transcriptional co-activator and downstream target of the Hippo/MST pathway in the biological processes of cell size control, proliferation and cell death[1], [2], [3], [>>13<<]. It has recently been shown that Mst1/2 ablation leads to hepatocellular carcinomas and the inhibition of YAP2 by MST kinases are an important mechanism in tumor suppression, especially in the progression of HCC (hepatocellular cancer)
n2:mentions
n3:19111660
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It has recently been shown that Mst1/2 ablation leads to hepatocellular carcinomas and the inhibition of YAP2 by MST kinases are an important mechanism in tumor suppression, especially in the progression of HCC (hepatocellular cancer) [>>14<<], [15], [16]. Interestingly, YAP2 was observed in nucleus in a panel of solid tumors, including liver, breast, ovary and prostate carcinomas [17], [18], [19], [20].
n2:mentions
n3:20545481
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recently been shown that Mst1/2 ablation leads to hepatocellular carcinomas and the inhibition of YAP2 by MST kinases are an important mechanism in tumor suppression, especially in the progression of HCC (hepatocellular cancer) [14], [>>15<<], [16]. Interestingly, YAP2 was observed in nucleus in a panel of solid tumors, including liver, breast, ovary and prostate carcinomas [17], [18], [19], [20].
n2:mentions
n3:19551889
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Interestingly, YAP2 was observed in nucleus in a panel of solid tumors, including liver, breast, ovary and prostate carcinomas [>>17<<], [18], [19], [20].
n2:mentions
n3:18953429
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Interestingly, YAP2 was observed in nucleus in a panel of solid tumors, including liver, breast, ovary and prostate carcinomas [17], [>>18<<], [19], [20].
n2:mentions
n3:18703216
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Interestingly, YAP2 was observed in nucleus in a panel of solid tumors, including liver, breast, ovary and prostate carcinomas [17], [18], [19], [>>20<<]. Together, these findings suggest that YAP2 functions as pro-survival factor and plays an important role in tumorigenesis. There is the striking conservation of Hippo pathway between Drosophila and mammals. Yki (Yorkie), the Drosophila
n2:mentions
n3:17974916
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Yki (Yorkie), the Drosophila orthologue of mammalian YAP2, promotes cell growth through transcriptionally co-activating Sd (Scalloped, Drosophila orthologue of mammalian TEAD) [>>1<<], [21], [22], [23], [24].
n2:mentions
n3:17889654
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Yki (Yorkie), the Drosophila orthologue of mammalian YAP2, promotes cell growth through transcriptionally co-activating Sd (Scalloped, Drosophila orthologue of mammalian TEAD) [1], [21], [>>22<<], [23], [24].
n2:mentions
n3:20368466
Subject Item
_:vb12486197
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Yki (Yorkie), the Drosophila orthologue of mammalian YAP2, promotes cell growth through transcriptionally co-activating Sd (Scalloped, Drosophila orthologue of mammalian TEAD) [1], [21], [22], [>>23<<], [24].
n2:mentions
n3:18258485
Subject Item
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Yki (Yorkie), the Drosophila orthologue of mammalian YAP2, promotes cell growth through transcriptionally co-activating Sd (Scalloped, Drosophila orthologue of mammalian TEAD) [1], [21], [22], [23], [>>24<<].
n2:mentions
n3:18258486
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The phosphorylation and ubiquitination of YAP2 has been reported [>>20<<], [25]. Recent studies showed that Lats phosphorylates YAP2 on serine 127 leading to its binding with 14-3-3 proteins [26], which results in cytoplasmic retention and transcriptional inhibition of YAP2.
n2:mentions
n3:17974916
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The phosphorylation and ubiquitination of YAP2 has been reported [20], [>>25<<]. Recent studies showed that Lats phosphorylates YAP2 on serine 127 leading to its binding with 14-3-3 proteins [26], which results in cytoplasmic retention and transcriptional inhibition of YAP2.
n2:mentions
n3:20048001
Subject Item
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Consistently, the S127A (serine replaced with alanine) mutation retains YAP2 in the nucleus and increases its transactivation, resulting in the cell overgrowth and the epithelial mesenchymal transition [>>27<<], [28]. Taken together, the phosphorylation and dephosphorylation of YAP2 dynamically regulates its biological function. However, the dephosphorylation of YAP2 remains unclear.
n2:mentions
n3:19935651
Subject Item
_:vb12486202
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Consistently, the S127A (serine replaced with alanine) mutation retains YAP2 in the nucleus and increases its transactivation, resulting in the cell overgrowth and the epithelial mesenchymal transition [27], [>>28<<]. Taken together, the phosphorylation and dephosphorylation of YAP2 dynamically regulates its biological function. However, the dephosphorylation of YAP2 remains unclear.
n2:mentions
n3:16894141
Subject Item
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The phosphoprotein phosphatase superfamily members include PP1, PP2A (PP2), PP2B (PP3), and PP4–7, among which PP1 is a major eukaryotic Ser/Thr protein phosphatase that involved in a variety of biological processes [>>29<<], [30]. TAZ, a mammalian YAP2 homologue [31], has been shown to be dephosphorylated by PP1A (catalytic subunit of PP1).
n2:mentions
n3:19879837
Subject Item
_:vb12486204
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n2:Context
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The phosphoprotein phosphatase superfamily members include PP1, PP2A (PP2), PP2B (PP3), and PP4–7, among which PP1 is a major eukaryotic Ser/Thr protein phosphatase that involved in a variety of biological processes [29], [>>30<<]. TAZ, a mammalian YAP2 homologue [31], has been shown to be dephosphorylated by PP1A (catalytic subunit of PP1).
n2:mentions
n3:1847640
Subject Item
_:vb12486205
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TAZ, a mammalian YAP2 homologue [>>31<<], has been shown to be dephosphorylated by PP1A (catalytic subunit of PP1).
n2:mentions
n3:19234525
Subject Item
_:vb12486206
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By cooperating with ASPP2 (apoptosis stimulating protein of p53-2), PP1A increases TAZ-mediated gene expression [>>32<<], [33]. Most recently it has been reported that α-catenin regulates Yap1 activity and phosphorylation by modulating its interaction with 14-3-3 proteins and PP2A phosphatase [34].
n2:mentions
n3:21189257
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By cooperating with ASPP2 (apoptosis stimulating protein of p53-2), PP1A increases TAZ-mediated gene expression [32], [>>33<<]. Most recently it has been reported that α-catenin regulates Yap1 activity and phosphorylation by modulating its interaction with 14-3-3 proteins and PP2A phosphatase [34].
n2:mentions
n3:21041411
Subject Item
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Most recently it has been reported that α-catenin regulates Yap1 activity and phosphorylation by modulating its interaction with 14-3-3 proteins and PP2A phosphatase [>>34<<].
n2:mentions
n3:21376238
Subject Item
_:vb12486209
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n5:Section
dc:title
materials and methods
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YAP2 shRNA targeting sequence: GACAUCUUCUGGUCAGAGA [>>13<<], the sequence was cloned into Ad Basic vector under U6 promoter.
n2:mentions
n3:19111660
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TAP assay has been previously described [>>42<<], [43]. Briefly, 4 liters of suspension HeLa cells that stably transfected with pOZ-FLAG-HA-YAP2 were harvested in 50 ml hypotonic buffer (1M Tris-HCl pH 7.3, 3M KCl, 1M MgCl2) containing protease and phosphatase inhibitors.
n2:mentions
n3:10504710
Subject Item
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TAP assay has been previously described [42], [>>43<<]. Briefly, 4 liters of suspension HeLa cells that stably transfected with pOZ-FLAG-HA-YAP2 were harvested in 50 ml hypotonic buffer (1M Tris-HCl pH 7.3, 3M KCl, 1M MgCl2) containing protease and phosphatase inhibitors.
n2:mentions
n3:11403571
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The precipitated proteins from TAP were centrifuged in 10%–40% gels as described [>>44<<].
n2:mentions
n3:17431397
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reactions were carried out by incubating immunprecipitated Lats and the recombinant GST-YAP2 for 30 min at 30°C in the presence of 3 µM cold ATP in 30 µl of buffer containing 20 mM HEPES (pH 7.4), 10 mM MgCl2, 10 mM MnCl2, 1 mM DTT [>>45<<]. In vitro dephosphorylation assay was performed by incubating the kinase reaction mixture with the recombinant GST-PP1 or GST only protein for 1 hour at 37°C in buffer containing 50 mM HEPES, 100 mM NaCl, 1 mM MnCl2, 2 mM DTT, 0.1 mM EGTA
n2:mentions
n3:21212262
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Luciferase activity was measured as described [>>23<<] according to the manufacturer's guidelines. HeLa cells were cultured in 24-well plates.
n2:mentions
n3:18258485
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results and discussion
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_:vb12486220 _:vb12486221 _:vb12486222 _:vb12486223 _:vb12486217 _:vb12486218 _:vb12486219 _:vb12486228 _:vb12486229 _:vb12486230 _:vb12486231 _:vb12486224 _:vb12486225 _:vb12486226 _:vb12486227 _:vb12486236 _:vb12486237 _:vb12486238 _:vb12486232 _:vb12486233 _:vb12486234 _:vb12486235
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By mass spectrometry analysis, we identified several known YAP2-interacting proteins including Lats1/2, AMOTL1/2, ASPP1/2 and TEAD1-4 [>>35<<], [36], [37] in the cytoplasmic or nuclear fraction (Figure 1B).
n2:mentions
n3:21205866
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_:vb12486218
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By mass spectrometry analysis, we identified several known YAP2-interacting proteins including Lats1/2, AMOTL1/2, ASPP1/2 and TEAD1-4 [35], [>>36<<], [37] in the cytoplasmic or nuclear fraction (Figure 1B).
n2:mentions
n3:21187284
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_:vb12486219
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By mass spectrometry analysis, we identified several known YAP2-interacting proteins including Lats1/2, AMOTL1/2, ASPP1/2 and TEAD1-4 [35], [36], [>>37<<] in the cytoplasmic or nuclear fraction (Figure 1B).
n2:mentions
n3:21041411
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Protein kinase Lats phosphorylates YAP2 at serine 127 and increases its association with 14-3-3 proteins, which leads to the cytoplasmic translocation and transcriptional inhibition of YAP2 [>>3<<], [38]. Due to the fact that phosphatase PP1A was identified as a YAP2 interacting protein, we asked whether YAP2 could be dephosphorylated by PP1.
n2:mentions
n3:12535517
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Protein kinase Lats phosphorylates YAP2 at serine 127 and increases its association with 14-3-3 proteins, which leads to the cytoplasmic translocation and transcriptional inhibition of YAP2 [3], [>>38<<]. Due to the fact that phosphatase PP1A was identified as a YAP2 interacting protein, we asked whether YAP2 could be dephosphorylated by PP1.
n2:mentions
n3:19900439
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It has been reported that serine 127 phosphorylation of YAP2 leads to the 14-3-3 binding and cytoplasmic translocation [>>3<<], [38]. It has been shown that 14-3-3 binding plays an important role in the regulation of YAP2 subcellular localization [38].
n2:mentions
n3:12535517
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It has been reported that serine 127 phosphorylation of YAP2 leads to the 14-3-3 binding and cytoplasmic translocation [3], [>>38<<]. It has been shown that 14-3-3 binding plays an important role in the regulation of YAP2 subcellular localization [38].
n2:mentions
n3:19900439
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It has been shown that 14-3-3 binding plays an important role in the regulation of YAP2 subcellular localization [>>38<<]. We examined the role of the PP1-mediated dephosphorylation of YAP2 in the inhibition of YAP2's interaction with 14-3-3 proteins. While expression of PP1A robustly disrupted the interaction of 14-3-3 proteins with YAP2 (Figure 3A),
n2:mentions
n3:19900439
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We took advantage of 3*Sd-LUC reporter system [>>23<<] to examine the effect of PP1 expression on the YAP2 co-transcriptional activity.
n2:mentions
n3:18258485
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CTGF (connective tissue growth factor) is one of the putative YAP2-TEAD target genes [>>35<<], [36], [37].
n2:mentions
n3:21205866
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CTGF (connective tissue growth factor) is one of the putative YAP2-TEAD target genes [35], [>>36<<], [37]. PP1A expression further increased YAP2-mediated upregulation of CTGF expression in quantative-RT-PCR assays (Figure 4B). Taken together, PP1A increases the YAP2-mediated transcriptional activation.
n2:mentions
n3:21187284
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CTGF (connective tissue growth factor) is one of the putative YAP2-TEAD target genes [35], [36], [>>37<<]. PP1A expression further increased YAP2-mediated upregulation of CTGF expression in quantative-RT-PCR assays (Figure 4B). Taken together, PP1A increases the YAP2-mediated transcriptional activation.
n2:mentions
n3:21041411
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It has been demonstrated that YAP functions as an oncoprotein in a panel of cancers including ovarian, breast and prostate cancer [>>17<<], [18], [19], [20]. In according with those findings, expression of YAP2 protected A2780 cells from cisplatin-induced cell death (Figure 4C).
n2:mentions
n3:18953429
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It has been demonstrated that YAP functions as an oncoprotein in a panel of cancers including ovarian, breast and prostate cancer [17], [>>18<<], [19], [20]. In according with those findings, expression of YAP2 protected A2780 cells from cisplatin-induced cell death (Figure 4C).
n2:mentions
n3:18703216
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It has been demonstrated that YAP functions as an oncoprotein in a panel of cancers including ovarian, breast and prostate cancer [17], [18], [19], [>>20<<]. In according with those findings, expression of YAP2 protected A2780 cells from cisplatin-induced cell death (Figure 4C).
n2:mentions
n3:17974916
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Since multiple lines of evidences have demonstrated that Hippo/MST-Yki/YAP2 signaling is conserved in mammals and Drosophila [>>1<<], an important goal of future studies is to determine whether Yki is regulated by PP1 in Drosophila.
n2:mentions
n3:17889654
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In agreement with the findings that Yap1 and TAZ are dephosphorylated and activated by PP2 and PP1, respectively [>>39<<], [40], we elucidate that PP1 dephosphorylates YAP2 at serine 127. However, it has been reported that there are multiple phosphorylation sites on YAP2 proteins induced by Lats or CK (Creatine kinase) kinase [41].
n2:mentions
n3:21189257
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In agreement with the findings that Yap1 and TAZ are dephosphorylated and activated by PP2 and PP1, respectively [39], [>>40<<], we elucidate that PP1 dephosphorylates YAP2 at serine 127. However, it has been reported that there are multiple phosphorylation sites on YAP2 proteins induced by Lats or CK (Creatine kinase) kinase [41].
n2:mentions
n3:21376238
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However, it has been reported that there are multiple phosphorylation sites on YAP2 proteins induced by Lats or CK (Creatine kinase) kinase [>>41<<]. CK phosphorylates YAP2 and induces its degradation via TrCP [41]. Our findings also raise the possibility that PP1 might be involved in the removal of other phosphorylation sites, namely the CK-mediated phosphorylation, and inhibit the
n2:mentions
n3:20048001
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CK phosphorylates YAP2 and induces its degradation via TrCP [>>41<<]. Our findings also raise the possibility that PP1 might be involved in the removal of other phosphorylation sites, namely the CK-mediated phosphorylation, and inhibit the protein degradation of YAP2.
n2:mentions
n3:20048001
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Tight junction related proteins, such as AMOLTL1/2 and Patj, have been shown to modulate YAP2 function in the process of cellular proliferation and homeostasis [>>35<<], [36]. Given the fact that PP1A and YAP2 forms a physical complex together with other appreciated YAP2 interacting proteins including tight junction related proteins, it will be interesting to investigate how protein phosphatase PP1
n2:mentions
n3:21205866
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Tight junction related proteins, such as AMOLTL1/2 and Patj, have been shown to modulate YAP2 function in the process of cellular proliferation and homeostasis [35], [>>36<<]. Given the fact that PP1A and YAP2 forms a physical complex together with other appreciated YAP2 interacting proteins including tight junction related proteins, it will be interesting to investigate how protein phosphatase PP1 regulates
n2:mentions
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