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10.1126/science.aac7906 http://scihub22266oqcxt.onion/10.1126/science.aac7906 C4727825!4727825!26339030     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 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 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Science 2015 ; 349 (6252): 1111-4 Nephropedia Template TP {{tp|p=26339030|t=2015. A direct role for the Sec1-Munc18-family protein Vps33 as a template for SNARE assembly |pdf=|usr=}}{{26339030}} gab.com Text A direct role for the Sec1-Munc18-family protein Vps33 as a template for SNARE assembly JO: Science http://www.kidney.de/pget.php?&tw=1&pmid=26339030 #FOAvip Fusion of intracellular transport vesicles requires soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs) and Sec1/Munc18-family (SM) proteins. Membrane-bridging SNARE complexes are critical for fusion, but their spontaneous assembly is inefficient and may require SM proteins in vivo. We report x-ray structures of Vps33, the SM subunit of the yeast vacuolar homotypic fusion and vacuole protein sorting (HOPS) complex, bound to two individual SNAREs. The two SNAREs, one from each membrane, are held in the correct orientation and register for subsequent complex assembly. Vps33 and potentially other SM proteins could thus act as templates for generating partially zipped SNARE assembly intermediates. HOPS was essential to mediate SNARE complex assembly at physiological SNARE concentrations. Thus, Vps33 appears to catalyze SNARE complex assembly through specific SNARE motif recognition. Twit Text FOAVip A direct role for the Sec1-Munc18-family protein Vps33 as a template for SNARE assembly ????Science http://www.kidney.de/pget.php?&tw=1&pmid=26339030 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26339030 #FOAvip English Wikipedia <ref>{{Cite pmid|26339030}}</ref> A direct role for the Sec1-Munc18-family protein Vps33 as a template for SNARE assembly #MMPMID26339030 Baker RW; Jeffrey PD; Zick M; Phillips BP; Wickner WT; Hughson FM Science 2015[Sep]; 349 (6252): 1111-4 PMID26339030show ga Fusion of intracellular transport vesicles requires soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs) and Sec1/Munc18-family (SM) proteins. Membrane-bridging SNARE complexes are critical for fusion, but their spontaneous assembly is inefficient and may require SM proteins in vivo. We report x-ray structures of Vps33, the SM subunit of the yeast vacuolar homotypic fusion and vacuole protein sorting (HOPS) complex, bound to two individual SNAREs. The two SNAREs, one from each membrane, are held in the correct orientation and register for subsequent complex assembly. Vps33 and potentially other SM proteins could thus act as templates for generating partially zipped SNARE assembly intermediates. HOPS was essential to mediate SNARE complex assembly at physiological SNARE concentrations. Thus, Vps33 appears to catalyze SNARE complex assembly through specific SNARE motif recognition. äA direct role for the Sec1-Munc18-family protein Vps33 as a template f(epmc).pdf DeepDyve Pubget Overpricing