Mechanical unzipping and rezipping of a single SNARE complex reveals hysteresis as a force-generating mechanism

Authors
Min, DuyoungKim, KipomHyeon, ChangbongCho, Yong HoonShin, Yeon-KyunYoon, Tae-Young
Issue Date
2013-04
Publisher
NATURE PUBLISHING GROUP
Citation
NATURE COMMUNICATIONS, v.4
Abstract
Formation of the soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complex provides mechanical thrust for membrane fusion, but its molecular mechanism is still unclear. Here using magnetic tweezers, we observe mechanical responses of a single neuronal SNARE complex under constant pulling force. Single SNARE complexes may be unzipped with 34 pN force. When rezipping is induced by lowering the force to 11 pN, only a partially assembled state results, with the C-terminal half of the SNARE complex remaining disassembled. Reassembly of the C-terminal half occurs only when the force is further lowered below 11 pN. Thus, mechanical hysteresis, characterized by the unzipping and rezipping cycle of a single SNARE complex, produces the partially assembled state. In this metastable state, unzipping toward the N-terminus is suppressed while zippering toward the C-terminus is initiated as a steep function of force. This ensures the directionality of SNARE-complex formation, making the SNARE complex a robust force-generating machine.
Keywords
MAGNETIC TWEEZERS; VESICLE FUSION; SYNAPTOBREVIN; DNA; MICROMANIPULATION; SYNAPTOTAGMIN-1; DYNAMICS; BINDING; MAGNETIC TWEEZERS; VESICLE FUSION; SYNAPTOBREVIN; DNA; MICROMANIPULATION; SYNAPTOTAGMIN-1; DYNAMICS; BINDING; Biological sciences; Biophysics; Cell biology
ISSN
2041-1723
URI
https://pubs.kist.re.kr/handle/201004/128217
DOI
10.1038/ncomms2692
Appears in Collections:
KIST Article > 2013
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