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10.1093/jmcb/mjv056 http://scihub22266oqcxt.onion/10.1093/jmcb/mjv056 C5943672!5943672!26450989     free     free     free Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       J+Mol+Cell+Biol 2016 ; 8 (1): 17-30 Nephropedia Template TP {{tp|p=26450989|t=2016. SUMOylation regulates p27Kip1 stability and localization in response to TGF? |pdf=|usr=}}{{26450989}} gab.com Text SUMOylation regulates p27Kip1 stability and localization in response to TGF JO: J Mol Cell Biol http://www.kidney.de/pget.php?&tw=1&pmid=26450989 #FOAvip Exposure of normal and tumor-derived cells to TGF? results in different outcomes, depending on the regulation of key targets. The CDK inhibitor p27Kip1 is one of these TGF? targets and is essential for the TGF?-induced cell cycle arrest. TGF? treatment inhibits p27Kip1 degradation and induces its nuclear translocation, through mechanisms that are still unknown. Recent evidences suggest that SUMOylation, a post-translational modification able to modulate the stability and subcellular localization of target proteins, critically modifies members of the TGF? signaling pathway. Here, we demonstrate that p27Kip1 is SUMOylated in response to TGF? treatment. Using different p27Kip1 point mutants, we identified lysine 134 (K134) as the residue modified by small ubiquitin-like modifier 1 (SUMO1) in response to TGF? treatment. TGF?-induced K134 SUMOylation increased protein stability and nuclear localization of both endogenous and exogenously expressed p27Kip1. We observed that SUMOylation regulated p27Kip1 binding to CDK2, thereby governing its nuclear proteasomal degradation through the phosphorylation of threonine 187. Importantly, p27Kip1 SUMOylation was necessary for proper cell cycle exit following TGF? treatment. These data indicate that SUMOylation is a novel regulatory mechanism that modulates p27Kip1 function in response to TGF? stimulation. Given the involvement of TGF? signaling in cancer cell proliferation and invasion, our data may shed light on an important aspect of this pathway during tumor progression. Twit Text FOAVip SUMOylation regulates p27Kip1 stability and localization in response to TGF ????J Mol Cell Biol http://www.kidney.de/pget.php?&tw=1&pmid=26450989 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26450989 #FOAvip English Wikipedia <ref>{{Cite pmid|26450989}}</ref> SUMOylation regulates p27Kip1 stability and localization in response to TGF? #MMPMID26450989 Lovisa S; Citro S; Sonego M; Dall'Acqua A; Ranzuglia V; Berton S; Colombatti A; Belletti B; Chiocca S; Schiappacassi M; Baldassarre G J Mol Cell Biol 2016[Feb]; 8 (1): 17-30 PMID26450989show ga Exposure of normal and tumor-derived cells to TGF? results in different outcomes, depending on the regulation of key targets. The CDK inhibitor p27Kip1 is one of these TGF? targets and is essential for the TGF?-induced cell cycle arrest. TGF? treatment inhibits p27Kip1 degradation and induces its nuclear translocation, through mechanisms that are still unknown. Recent evidences suggest that SUMOylation, a post-translational modification able to modulate the stability and subcellular localization of target proteins, critically modifies members of the TGF? signaling pathway. Here, we demonstrate that p27Kip1 is SUMOylated in response to TGF? treatment. Using different p27Kip1 point mutants, we identified lysine 134 (K134) as the residue modified by small ubiquitin-like modifier 1 (SUMO1) in response to TGF? treatment. TGF?-induced K134 SUMOylation increased protein stability and nuclear localization of both endogenous and exogenously expressed p27Kip1. We observed that SUMOylation regulated p27Kip1 binding to CDK2, thereby governing its nuclear proteasomal degradation through the phosphorylation of threonine 187. Importantly, p27Kip1 SUMOylation was necessary for proper cell cycle exit following TGF? treatment. These data indicate that SUMOylation is a novel regulatory mechanism that modulates p27Kip1 function in response to TGF? stimulation. Given the involvement of TGF? signaling in cancer cell proliferation and invasion, our data may shed light on an important aspect of this pathway during tumor progression. äSUMOylation regulates p27Kip1 stability and localization in response t(epmc).pdf DeepDyve Pubget Overpricing