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10.1038/ncomms2244 http://scihub22266oqcxt.onion/10.1038/ncomms2244 23212369!3526956!23212369     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=23212369&cmd=llinks): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 215 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Nat+Commun 2012 ; 3 (ä): 1240 Nephropedia Template TP {{tp|p=23212369|t=2012. Molecular determinants of selective clearance of protein inclusions by autophagy |pdf=|usr=}}{{23212369}} gab.com Text Molecular determinants of selective clearance of protein inclusions by autophagy JO: Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=23212369 #FOAvip Protein quality control is essential for cellular survival. Failure to eliminate pathogenic proteins leads to their intracellular accumulation in the form of protein aggregates. Autophagy can recognize protein aggregates and degrade them in lysosomes. However, some aggregates escape the autophagic surveillance. Here we analyse the autophagic degradation of different types of aggregates of synphilin-1, a protein often found in pathogenic protein inclusions. We show that small synphilin-1 aggregates and large aggresomes are differentially targeted by constitutive and inducible autophagy. Furthermore, we identify a region in synphilin-1, necessary for its own basal and inducible aggrephagy and sufficient for the degradation of other pro-aggregating proteins. Although the presence of this peptide is sufficient for basal aggrephagy, inducible aggrephagy requires its ubiquitination, which diminishes protein mobility on the surface of the aggregate and favours the recruitment and assembly of the protein complexes required for autophagosome formation. Our study reveals different mechanisms for cells to cope with aggregate proteins via autophagy and supports the idea that autophagic susceptibility of prone-to-aggregate proteins may not depend on the nature of the aggregating proteins per se, but on their dynamic properties in the aggregate. Twit Text FOAVip Molecular determinants of selective clearance of protein inclusions by autophagy ????Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=23212369 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=23212369 #FOAvip English Wikipedia <ref>{{Cite pmid|23212369}}</ref> Molecular determinants of selective clearance of protein inclusions by autophagy #MMPMID23212369 Wong E; Bejarano E; Rakshit M; Lee K; Hanson HH; Zaarur N; Phillips GR; Sherman MY; Cuervo AM Nat Commun 2012[]; 3 (ä): 1240 PMID23212369show ga Protein quality control is essential for cellular survival. Failure to eliminate pathogenic proteins leads to their intracellular accumulation in the form of protein aggregates. Autophagy can recognize protein aggregates and degrade them in lysosomes. However, some aggregates escape the autophagic surveillance. Here we analyse the autophagic degradation of different types of aggregates of synphilin-1, a protein often found in pathogenic protein inclusions. We show that small synphilin-1 aggregates and large aggresomes are differentially targeted by constitutive and inducible autophagy. Furthermore, we identify a region in synphilin-1, necessary for its own basal and inducible aggrephagy and sufficient for the degradation of other pro-aggregating proteins. Although the presence of this peptide is sufficient for basal aggrephagy, inducible aggrephagy requires its ubiquitination, which diminishes protein mobility on the surface of the aggregate and favours the recruitment and assembly of the protein complexes required for autophagosome formation. Our study reveals different mechanisms for cells to cope with aggregate proteins via autophagy and supports the idea that autophagic susceptibility of prone-to-aggregate proteins may not depend on the nature of the aggregating proteins per se, but on their dynamic properties in the aggregate. |Ankyrins/physiology[MESH] |Autophagy/*physiology[MESH] |Carrier Proteins/metabolism[MESH] |Cell Line[MESH] |Cell Physiological Phenomena/physiology[MESH] |Inclusion Bodies/metabolism[MESH] |Intracellular Signaling Peptides and Proteins[MESH] |Nerve Tissue Proteins/metabolism[MESH] |Peptides/metabolism/physiology[MESH] |Phagosomes/metabolism/physiology[MESH] |Proteins/*metabolism/physiology[MESH]Molecular determinants of selective clearance of protein inclusions by(epmc).pdf DeepDyve Pubget Overpricing