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10.1073/pnas.1611506114

http://scihub22266oqcxt.onion/10.1073/pnas.1611506114
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C5448213!5448213!28490503
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suck abstract from ncbi


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pmid28490503      Proc+Natl+Acad+Sci+U+S+A 2017 ; 114 (21): 5455-60
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  • 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): 5455-60 PMID28490503show ga
  • Secretion of neurotransmitters and hormones depends on membrane fusion, accomplished by a cellular fusion machinery whose core components are SNARE proteins. Several vesicle-associated v-SNAREs form SNAREpin complexes with target membrane-associated t-SNAREs, but how they cooperate to catalyze fusion is unknown. Using highly coarse-grained simulations, we found that steric interactions spontaneously organized SNAREpins into circular clusters, expanded the clusters, and forced membranes together. These are entropic effects, reminiscent of cooperative transitions in solutions of rod-like molecules. The rate of fusion was controlled by the number of SNAREs, because more SNAREs generated greater entropic forces. Given ?70 v-SNAREs available per synaptic vesicle, entropic cooperativity among SNAREpins may underlie the sub-millisecond timescale of neurotransmitter release.
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