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10.1016/j.cell.2016.07.001 http://scihub22266oqcxt.onion/10.1016/j.cell.2016.07.001 C5003816!5003816!27477512     free     free     free Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Cell 2016 ; 166 (4): 935-49 Nephropedia Template TP {{tp|p=27477512|t=2016. UBQLN2 Mediates Autophagy-Independent Protein Aggregate Clearance by the Proteasome |pdf=|usr=}}{{27477512}} gab.com Text UBQLN2 Mediates Autophagy-Independent Protein Aggregate Clearance by the Proteasome JO: Cell http://www.kidney.de/pget.php?&tw=1&pmid=27477512 #FOAvip Clearance of misfolded and aggregated proteins is central to cell survival. Here, we describe a new pathway for maintaining protein homeostasis mediated by the proteasome shuttle factor UBQLN2. The 26S proteasome degrades polyubiquitylated substrates by recognizing them through stoichiometrically bound ubiquitin receptors, but substrates are also delivered by reversibly bound shuttles. We aimed to determine why these parallel delivery mechanisms exist and found that UBQLN2 acts with the HSP70-HSP110 disaggregase machinery to clear protein aggregates via the 26S proteasome. UBQLN2 recognizes client-bound HSP70 and links it to the proteasome to allow for the degradation of aggregated and misfolded proteins. We further show that this process is active in the cell nucleus, where another system for aggregate clearance, autophagy, does not act. Finally, we found that mutations in UBQLN2, which lead to neurodegeneration in humans, are defective in chaperone binding, impair aggregate clearance, and cause cognitive deficits in mice. Twit Text FOAVip UBQLN2 Mediates Autophagy-Independent Protein Aggregate Clearance by the Proteasome ????Cell http://www.kidney.de/pget.php?&tw=1&pmid=27477512 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27477512 #FOAvip English Wikipedia <ref>{{Cite pmid|27477512}}</ref> UBQLN2 Mediates Autophagy-Independent Protein Aggregate Clearance by the Proteasome #MMPMID27477512 Hjerpe R; Bett J; Keuss M; Solovyova A; McWilliams T; Johnson C; Sahu I; Varghese J; Wood N; Wightman M; Osborne G; Bates G; Glickman M; Trost M; Knebel A; Marchesi F; Kurz T Cell 2016[Aug]; 166 (4): 935-49 PMID27477512show ga Clearance of misfolded and aggregated proteins is central to cell survival. Here, we describe a new pathway for maintaining protein homeostasis mediated by the proteasome shuttle factor UBQLN2. The 26S proteasome degrades polyubiquitylated substrates by recognizing them through stoichiometrically bound ubiquitin receptors, but substrates are also delivered by reversibly bound shuttles. We aimed to determine why these parallel delivery mechanisms exist and found that UBQLN2 acts with the HSP70-HSP110 disaggregase machinery to clear protein aggregates via the 26S proteasome. UBQLN2 recognizes client-bound HSP70 and links it to the proteasome to allow for the degradation of aggregated and misfolded proteins. We further show that this process is active in the cell nucleus, where another system for aggregate clearance, autophagy, does not act. Finally, we found that mutations in UBQLN2, which lead to neurodegeneration in humans, are defective in chaperone binding, impair aggregate clearance, and cause cognitive deficits in mice. äUBQLN2 Mediates Autophagy-Independent Protein Aggregate Clearance by t(epmc).pdf DeepDyve Pubget Overpricing