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10.1073/pnas.1611506114 http://scihub22266oqcxt.onion/10.1073/pnas.1611506114 C5448213!5448213 !28490503     free     free     free Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\28490503 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Proc+Natl+Acad+Sci+U+S+A 2017 ; 114 (21 ): 5455-5460 Nephropedia Template TP {{tp|p=28490503 |t=2017. Entropic forces drive self-organization and membrane fusion by SNARE proteins |pdf=|usr=}}{{28490503 }} gab.com Text Entropic forces drive self-organization and membrane fusion by SNARE proteins JO: Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=28490503 #FOAvip SNARE proteins are the core of the cell's fusion machinery and mediate virtually all known intracellular membrane fusion reactions on which exocytosis and trafficking depend. Fusion is catalyzed when vesicle-associated v-SNAREs form trans-SNARE complexes ("SNAREpins") with target membrane-associated t-SNAREs, a zippering-like process releasing ?65 kT per SNAREpin. Fusion requires several SNAREpins, but how they cooperate is unknown and reports of the number required vary widely. To capture the collective behavior on the long timescales of fusion, we developed a highly coarse-grained model that retains key biophysical SNARE properties such as the zippering energy landscape and the surface charge distribution. In simulations the ?65-kT zippering energy was almost entirely dissipated, with fully assembled SNARE motifs but uncomplexed linker domains. The SNAREpins self-organized into a circular cluster at the fusion site, driven by entropic forces that originate in steric-electrostatic interactions among SNAREpins and membranes. Cooperative entropic forces expanded the cluster and pulled the membranes together at the center point with high force. We find that there is no critical number of SNAREs required for fusion, but instead the fusion rate increases rapidly with the number of SNAREpins due to increasing entropic forces. We hypothesize that this principle finds physiological use to boost fusion rates to meet the demanding timescales of neurotransmission, exploiting the large number of v-SNAREs available in synaptic vesicles. Once in an unfettered cluster, we estimate ?15 SNAREpins are required for fusion within the ?1-ms timescale of neurotransmitter release. Twit Text FOAVip Entropic forces drive self-organization and membrane fusion by SNARE proteins ????Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=28490503 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28490503 #FOAvip English Wikipedia <ref>{{Cite pmid|28490503 }}</ref> Entropic forces drive self-organization and membrane fusion by SNARE proteins #MMPMID28490503 Mostafavi H ; Thiyagarajan S ; Stratton BS ; Karatekin E ; Warner JM ; Rothman JE ; O'Shaughnessy B Proc Natl Acad Sci U S A 2017[May]; 114 (21 ): 5455-5460 PMID28490503 show ga SNARE proteins are the core of the cell's fusion machinery and mediate virtually all known intracellular membrane fusion reactions on which exocytosis and trafficking depend. Fusion is catalyzed when vesicle-associated v-SNAREs form trans-SNARE complexes ("SNAREpins") with target membrane-associated t-SNAREs, a zippering-like process releasing ?65 kT per SNAREpin. Fusion requires several SNAREpins, but how they cooperate is unknown and reports of the number required vary widely. To capture the collective behavior on the long timescales of fusion, we developed a highly coarse-grained model that retains key biophysical SNARE properties such as the zippering energy landscape and the surface charge distribution. In simulations the ?65-kT zippering energy was almost entirely dissipated, with fully assembled SNARE motifs but uncomplexed linker domains. The SNAREpins self-organized into a circular cluster at the fusion site, driven by entropic forces that originate in steric-electrostatic interactions among SNAREpins and membranes. Cooperative entropic forces expanded the cluster and pulled the membranes together at the center point with high force. We find that there is no critical number of SNAREs required for fusion, but instead the fusion rate increases rapidly with the number of SNAREpins due to increasing entropic forces. We hypothesize that this principle finds physiological use to boost fusion rates to meet the demanding timescales of neurotransmission, exploiting the large number of v-SNAREs available in synaptic vesicles. Once in an unfettered cluster, we estimate ?15 SNAREpins are required for fusion within the ?1-ms timescale of neurotransmitter release. |*Exocytosis [MESH] |*Membrane Fusion [MESH] |*Models, Biological [MESH] |Entropy [MESH] |Monte Carlo Method [MESH]Entropic forces drive self-organization and membrane fusion by SNARE p(epmc).pdf DeepDyve Pubget Overpricing