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10.1016/j.celrep.2017.03.030 http://scihub22266oqcxt.onion/10.1016/j.celrep.2017.03.030 C5395095!5395095!28380357     free     free     free Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\28380357.jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Cell+Rep 2017 ; 19 (1): 188-202 Nephropedia Template TP {{tp|p=28380357|t=2017. Keap1/Cullin3 Modulates p62/SQSTM1 Activity via UBA domain Ubiquitination |pdf=|usr=}}{{28380357}} gab.com Text Keap1/Cullin3 Modulates p62/SQSTM1 Activity via UBA domain Ubiquitination JO: Cell Rep http://www.kidney.de/pget.php?&tw=1&pmid=28380357 #FOAvip p62/SQSTM1 (p62) is a scaffolding protein that facilitates the formation and degradation of ubiquitinated aggregates via its self-interaction and ubiquitin binding domains. The regulation of this process is unclear but may relate to the post-translational modification of p62. In the present study, we find that Keap1/Cullin3 ubiquitinates p62 at lysine 420 within its UBA domain. Substitution of lysine 420 with an arginine diminishes p62 sequestration and degradation activity similar to that seen when the UBA domain is deleted. Overexpression of Keap1/Cullin3 in p62-WT expressing cells increases ubiquitinated inclusion formation, p62?s association with LC3 and rescues proteotoxicity. This effect is not seen in cells expressing a mutant p62 that fails to interact with Keap1. Interestingly, p62 disease mutants have diminished or absent UBA domain ubiquitination. These data suggest that the ubiquitination of p62?s UBA domain at lysine 420 may regulate p62?s function and be disrupted in p62 associated disease. Twit Text FOAVip Keap1/Cullin3 Modulates p62/SQSTM1 Activity via UBA domain Ubiquitination ????Cell Rep http://www.kidney.de/pget.php?&tw=1&pmid=28380357 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28380357 #FOAvip English Wikipedia <ref>{{Cite pmid|28380357}}</ref> Keap1/Cullin3 Modulates p62/SQSTM1 Activity via UBA domain Ubiquitination #MMPMID28380357 Lee Y; Chou TF; Pittman SK; Keith AL; Razani B; Weihl CC Cell Rep 2017[Apr]; 19 (1): 188-202 PMID28380357show ga p62/SQSTM1 (p62) is a scaffolding protein that facilitates the formation and degradation of ubiquitinated aggregates via its self-interaction and ubiquitin binding domains. The regulation of this process is unclear but may relate to the post-translational modification of p62. In the present study, we find that Keap1/Cullin3 ubiquitinates p62 at lysine 420 within its UBA domain. Substitution of lysine 420 with an arginine diminishes p62 sequestration and degradation activity similar to that seen when the UBA domain is deleted. Overexpression of Keap1/Cullin3 in p62-WT expressing cells increases ubiquitinated inclusion formation, p62?s association with LC3 and rescues proteotoxicity. This effect is not seen in cells expressing a mutant p62 that fails to interact with Keap1. Interestingly, p62 disease mutants have diminished or absent UBA domain ubiquitination. These data suggest that the ubiquitination of p62?s UBA domain at lysine 420 may regulate p62?s function and be disrupted in p62 associated disease. äKeap1/Cullin3 Modulates p62/SQSTM1 Activity via UBA domain Ubiquitinat(epmc).pdf DeepDyve Pubget Overpricing