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10.1073/pnas.1504368112 http://scihub22266oqcxt.onion/10.1073/pnas.1504368112 C4403200!4403200!25825753     free     free     free Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Proc+Natl+Acad+Sci+U+S+A 2015 ; 112 (15): E1851-60 Nephropedia Template TP {{tp|p=25825753|t=2015. Cis and trans interactions between atlastin molecules during membrane fusion |pdf=|usr=}}{{25825753}} gab.com Text Cis and trans interactions between atlastin molecules during membrane fusion JO: Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=25825753 #FOAvip The membrane-anchored GTPase atlastin (ATL) mediates the fusion of endoplasmic reticulum membranes into a network of tubules and sheets, but the mechanism of ATL function is still poorly understood. Here we show that vesicle fusion is preceded by GTP hydrolysis-dependent tethering, caused by the interaction of ATL molecules in opposing membranes. GTP hydrolysis also dissociates ATL dimers sitting in the same membrane (cis dimers), generating a pool of ATL monomers that can dimerize with molecules on a different (trans) membrane. Multiple rounds of GTP hydrolysis and the cooperation of several ATL molecules in each membrane are required for a successful fusion event. These results lead to a model of ATL-mediated fusion that also may have implications for SNARE-mediated fusion. Twit Text FOAVip Cis and trans interactions between atlastin molecules during membrane fusion ????Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=25825753 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25825753 #FOAvip English Wikipedia <ref>{{Cite pmid|25825753}}</ref> Cis and trans interactions between atlastin molecules during membrane fusion #MMPMID25825753 Liu TY; Bian X; Romano FB; Shemesh T; Rapoport TA; Hu J Proc Natl Acad Sci U S A 2015[Apr]; 112 (15): E1851-60 PMID25825753show ga The membrane-anchored GTPase atlastin (ATL) mediates the fusion of endoplasmic reticulum membranes into a network of tubules and sheets, but the mechanism of ATL function is still poorly understood. Here we show that vesicle fusion is preceded by GTP hydrolysis-dependent tethering, caused by the interaction of ATL molecules in opposing membranes. GTP hydrolysis also dissociates ATL dimers sitting in the same membrane (cis dimers), generating a pool of ATL monomers that can dimerize with molecules on a different (trans) membrane. Multiple rounds of GTP hydrolysis and the cooperation of several ATL molecules in each membrane are required for a successful fusion event. These results lead to a model of ATL-mediated fusion that also may have implications for SNARE-mediated fusion. äCis and trans interactions between atlastin molecules during membrane (epmc).pdf DeepDyve Pubget Overpricing