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10.4161/auto.28980 http://scihub22266oqcxt.onion/10.4161/auto.28980 C4203560!4203560!24963637     free     free     free Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\24963637.jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Autophagy 2014 ; 10 (7): 1343-5 Nephropedia Template TP {{tp|p=24963637|t=2014. Scaffolding the expansion of autophagosomes |pdf=|usr=}}{{24963637}} gab.com Text Scaffolding the expansion of autophagosomes JO: Autophagy http://www.kidney.de/pget.php?&tw=1&pmid=24963637 #FOAvip The conjugation of the small ubiquitin (Ub)-like protein Atg8 to autophagic membranes is a key step during the expansion of phagophores. This reaction is driven by 2 interconnected Ub-like conjugation systems. The second system conjugates the Ub-like protein Atg12 to Atg5. The resulting conjugate catalyzes the covalent attachment of Atg8 to membranes. Atg12?Atg5, however, constitutively associates with the functionally less well-characterized coiled-coil protein Atg16. By reconstituting the conjugation of Atg8 to membranes in vitro, we showed that after Atg8 has been attached to phosphatidylethanolamine (PE), it recruits Atg12?Atg5 to membranes by recognizing a noncanonical Atg8-interacting motif (AIM) within Atg12. Atg16 crosslinks Atg8?PE-Atg12?Atg5 complexes to form a continuous 2-dimensional membrane scaffold with meshwork-like architecture. Apparently, scaffold formation is required to generate productive autophagosomes and to deliver autophagic cargo to the vacuole in vivo. Twit Text FOAVip Scaffolding the expansion of autophagosomes ????Autophagy http://www.kidney.de/pget.php?&tw=1&pmid=24963637 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=24963637 #FOAvip English Wikipedia <ref>{{Cite pmid|24963637}}</ref> Scaffolding the expansion of autophagosomes #MMPMID24963637 Kaufmann A; Wollert T Autophagy 2014[Jul]; 10 (7): 1343-5 PMID24963637show ga The conjugation of the small ubiquitin (Ub)-like protein Atg8 to autophagic membranes is a key step during the expansion of phagophores. This reaction is driven by 2 interconnected Ub-like conjugation systems. The second system conjugates the Ub-like protein Atg12 to Atg5. The resulting conjugate catalyzes the covalent attachment of Atg8 to membranes. Atg12?Atg5, however, constitutively associates with the functionally less well-characterized coiled-coil protein Atg16. By reconstituting the conjugation of Atg8 to membranes in vitro, we showed that after Atg8 has been attached to phosphatidylethanolamine (PE), it recruits Atg12?Atg5 to membranes by recognizing a noncanonical Atg8-interacting motif (AIM) within Atg12. Atg16 crosslinks Atg8?PE-Atg12?Atg5 complexes to form a continuous 2-dimensional membrane scaffold with meshwork-like architecture. Apparently, scaffold formation is required to generate productive autophagosomes and to deliver autophagic cargo to the vacuole in vivo. äScaffolding the expansion of autophagosomes (epmc).pdf DeepDyve Pubget Overpricing