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10.1016/j.cell.2014.07.050 http://scihub22266oqcxt.onion/10.1016/j.cell.2014.07.050 C4163015!4163015!25215493     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       Cell 2014 ; 158 (6): 1375-88 Nephropedia Template TP {{tp|p=25215493|t=2014. Key steps in ERAD of luminal ER proteins reconstituted with purified components |pdf=|usr=}}{{25215493}} gab.com Text Key steps in ERAD of luminal ER proteins reconstituted with purified components JO: Cell http://www.kidney.de/pget.php?&tw=1&pmid=25215493 #FOAvip Misfolded proteins of the endoplasmic reticulum (ER) are retro-translocated into the cytosol, poly-ubiquitinated, and degraded by the proteasome, a process called ER-associated protein degradation (ERAD). Here, we have used purified components from Saccharomyces cerevisiae to analyze the mechanism of retro-translocation of luminal substrates (ERAD-L), recapitulating key steps in a basic process where the ubiquitin ligase Hrd1p is the only required membrane protein. We show that Hrd1p interacts with substrate through its membrane-spanning domain, discriminating misfolded from folded polypeptides. Both Hrd1p and substrate are poly-ubiquitinated, resulting in the binding of the Cdc48p ATPase complex. Subsequently, ATP hydrolysis by Cdc48p releases substrate from Hrd1p. Finally, ubiquitin chains are trimmed by the de-ubiquitinating enzyme Otu1p, which is recruited and activated by the Cdc48p complex. Cdc48p-dependent membrane extraction of poly-ubiquitinated proteins can be reproduced with reconstituted proteoliposomes. Our results suggest a model for retro-translocation in which Hrd1p forms a membrane conduit for misfolded proteins. Twit Text FOAVip Key steps in ERAD of luminal ER proteins reconstituted with purified components ????Cell http://www.kidney.de/pget.php?&tw=1&pmid=25215493 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25215493 #FOAvip English Wikipedia <ref>{{Cite pmid|25215493}}</ref> Key steps in ERAD of luminal ER proteins reconstituted with purified components #MMPMID25215493 Stein A; Ruggiano A; Carvalho P; Rapoport TA Cell 2014[Sep]; 158 (6): 1375-88 PMID25215493show ga Misfolded proteins of the endoplasmic reticulum (ER) are retro-translocated into the cytosol, poly-ubiquitinated, and degraded by the proteasome, a process called ER-associated protein degradation (ERAD). Here, we have used purified components from Saccharomyces cerevisiae to analyze the mechanism of retro-translocation of luminal substrates (ERAD-L), recapitulating key steps in a basic process where the ubiquitin ligase Hrd1p is the only required membrane protein. We show that Hrd1p interacts with substrate through its membrane-spanning domain, discriminating misfolded from folded polypeptides. Both Hrd1p and substrate are poly-ubiquitinated, resulting in the binding of the Cdc48p ATPase complex. Subsequently, ATP hydrolysis by Cdc48p releases substrate from Hrd1p. Finally, ubiquitin chains are trimmed by the de-ubiquitinating enzyme Otu1p, which is recruited and activated by the Cdc48p complex. Cdc48p-dependent membrane extraction of poly-ubiquitinated proteins can be reproduced with reconstituted proteoliposomes. Our results suggest a model for retro-translocation in which Hrd1p forms a membrane conduit for misfolded proteins. äKey steps in ERAD of luminal ER proteins reconstituted with purified c(epmc).pdf DeepDyve Pubget Overpricing