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10.1074/jbc.M117.775700 http://scihub22266oqcxt.onion/10.1074/jbc.M117.775700 C5519362!5519362!28539358     free     free     free Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       J+Biol+Chem 2017 ; 292 (29): 12100-10 Nephropedia Template TP {{tp|p=28539358|t=2017. Protein kinase C ? stabilizes ?-catenin and regulates its subcellular localization in podocytes |pdf=|usr=}}{{28539358}} gab.com Text Protein kinase C stabilizes -catenin and regulates its subcellular localization in podocytes JO: J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=28539358 #FOAvip Kidney disease has been linked to dysregulated signaling via PKC in kidney cells such as podocytes. PKC? is a conventional isoform of PKC and a well-known binding partner of ?-catenin, which promotes its degradation. ?-Catenin is the main effector of the canonical Wnt pathway and is critical in cell adhesion. However, whether other PKC isoforms interact with ?-catenin has not been studied systematically. Here we demonstrate that PKC?-deficient mice, which develop proteinuria and glomerulosclerosis, display lower ?-catenin expression compared with PKC wild-type mice, consistent with an altered phenotype of podocytes in culture. Remarkably, ?-catenin showed a reversed subcellular localization pattern: Although ?-catenin exhibited a perinuclear pattern in undifferentiated wild-type cells, it predominantly localized to the nucleus in PKC? knockout cells. Phorbol 12-myristate 13-acetate stimulation of both cell types revealed that PKC? positively regulates ?-catenin expression and stabilization in a glycogen synthase kinase 3?-independent manner. Further, ?-catenin overexpression in PKC?-deficient podocytes could restore the wild-type phenotype, similar to rescue with a PKC? construct. This effect was mediated by up-regulation of P-cadherin and the ?-catenin downstream target fascin1. Zebrafish studies indicated three PKC?-specific phosphorylation sites in ?-catenin that are required for full ?-catenin function. Co-immunoprecipitation and pulldown assays confirmed PKC? and ?-catenin as binding partners and revealed that ablation of the three PKC? phosphorylation sites weakens their interaction. In summary, we identified a novel pathway for regulation of ?-catenin levels and define PKC? as an important ?-catenin interaction partner and signaling opponent of other PKC isoforms in podocytes. Twit Text FOAVip Protein kinase C stabilizes -catenin and regulates its subcellular localization in podocytes ????J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=28539358 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28539358 #FOAvip English Wikipedia <ref>{{Cite pmid|28539358}}</ref> Protein kinase C ? stabilizes ?-catenin and regulates its subcellular localization in podocytes #MMPMID28539358 Duong M; Yu X; Teng B; Schroder P; Haller H; Eschenburg S; Schiffer M J Biol Chem 2017[Jul]; 292 (29): 12100-10 PMID28539358show ga Kidney disease has been linked to dysregulated signaling via PKC in kidney cells such as podocytes. PKC? is a conventional isoform of PKC and a well-known binding partner of ?-catenin, which promotes its degradation. ?-Catenin is the main effector of the canonical Wnt pathway and is critical in cell adhesion. However, whether other PKC isoforms interact with ?-catenin has not been studied systematically. Here we demonstrate that PKC?-deficient mice, which develop proteinuria and glomerulosclerosis, display lower ?-catenin expression compared with PKC wild-type mice, consistent with an altered phenotype of podocytes in culture. Remarkably, ?-catenin showed a reversed subcellular localization pattern: Although ?-catenin exhibited a perinuclear pattern in undifferentiated wild-type cells, it predominantly localized to the nucleus in PKC? knockout cells. Phorbol 12-myristate 13-acetate stimulation of both cell types revealed that PKC? positively regulates ?-catenin expression and stabilization in a glycogen synthase kinase 3?-independent manner. Further, ?-catenin overexpression in PKC?-deficient podocytes could restore the wild-type phenotype, similar to rescue with a PKC? construct. This effect was mediated by up-regulation of P-cadherin and the ?-catenin downstream target fascin1. Zebrafish studies indicated three PKC?-specific phosphorylation sites in ?-catenin that are required for full ?-catenin function. Co-immunoprecipitation and pulldown assays confirmed PKC? and ?-catenin as binding partners and revealed that ablation of the three PKC? phosphorylation sites weakens their interaction. In summary, we identified a novel pathway for regulation of ?-catenin levels and define PKC? as an important ?-catenin interaction partner and signaling opponent of other PKC isoforms in podocytes. äProtein kinase C ? stabilizes ?-catenin and regulates its subcellular (epmc).pdf DeepDyve Pubget Overpricing