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10.15252/embr.201642209 http://scihub22266oqcxt.onion/10.15252/embr.201642209 C5090699!5090699!27644261     free     free     free Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 247.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       EMBO+Rep 2016 ; 17 (11): 1590-608 Nephropedia Template TP {{tp|p=27644261|t=2016. Steric hindrance of SNARE transmembrane domain organization impairs the hemifusion?to?fusion transition |pdf=|usr=}}{{27644261}} gab.com Text Steric hindrance of SNARE transmembrane domain organization impairs the hemifusion to fusion transition JO: EMBO Rep http://www.kidney.de/pget.php?&tw=1&pmid=27644261 #FOAvip SNAREs fuse membranes in several steps. Trans?SNARE complexes juxtapose membranes, induce hemifused stalk structures, and open the fusion pore. A recent penetration model of fusion proposed that SNAREs force the hydrophilic C?termini of their transmembrane domains through the hydrophobic core of the membrane(s). In contrast, the indentation model suggests that the C?termini open the pore by locally compressing and deforming the stalk. Here we test these models in the context of yeast vacuole fusion. Addition of small hydrophilic tags renders bilayer penetration by the C?termini energetically unlikely. It preserves fusion activity, however, arguing against the penetration model. Addition of large protein tags to the C?termini permits SNARE activation, trans?SNARE pairing, and hemifusion but abolishes pore opening. Fusion proceeds if the tags are detached from the membrane by a hydrophilic spacer or if only one side of the trans?SNARE complex carries a protein tag. Thus, both sides of a trans?SNARE complex can drive pore opening. Our results are consistent with an indentation model in which multiple SNARE C?termini cooperate in opening the fusion pore by locally deforming the inner leaflets. Twit Text FOAVip Steric hindrance of SNARE transmembrane domain organization impairs the hemifusion to fusion transition ????EMBO Rep http://www.kidney.de/pget.php?&tw=1&pmid=27644261 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27644261 #FOAvip English Wikipedia <ref>{{Cite pmid|27644261}}</ref> Steric hindrance of SNARE transmembrane domain organization impairs the hemifusion?to?fusion transition #MMPMID27644261 D'Agostino M; Risselada HJ; Mayer A EMBO Rep 2016[Nov]; 17 (11): 1590-608 PMID27644261show ga SNAREs fuse membranes in several steps. Trans?SNARE complexes juxtapose membranes, induce hemifused stalk structures, and open the fusion pore. A recent penetration model of fusion proposed that SNAREs force the hydrophilic C?termini of their transmembrane domains through the hydrophobic core of the membrane(s). In contrast, the indentation model suggests that the C?termini open the pore by locally compressing and deforming the stalk. Here we test these models in the context of yeast vacuole fusion. Addition of small hydrophilic tags renders bilayer penetration by the C?termini energetically unlikely. It preserves fusion activity, however, arguing against the penetration model. Addition of large protein tags to the C?termini permits SNARE activation, trans?SNARE pairing, and hemifusion but abolishes pore opening. Fusion proceeds if the tags are detached from the membrane by a hydrophilic spacer or if only one side of the trans?SNARE complex carries a protein tag. Thus, both sides of a trans?SNARE complex can drive pore opening. Our results are consistent with an indentation model in which multiple SNARE C?termini cooperate in opening the fusion pore by locally deforming the inner leaflets. äSteric hindrance of SNARE transmembrane domain organization impairs th(epmc).pdf DeepDyve Pubget Overpricing