DC Field | Value | Language |
---|---|---|
dc.contributor.author | Min, Duyoung | ko |
dc.contributor.author | Kim, Kipom | ko |
dc.contributor.author | Hyeon, Changbong | ko |
dc.contributor.author | Cho, Yong-Hoon | ko |
dc.contributor.author | Shin, Yeon-Kyun | ko |
dc.contributor.author | Yoon, Tae-Young | ko |
dc.date.accessioned | 2017-08-08T06:41:40Z | - |
dc.date.available | 2017-08-08T06:41:40Z | - |
dc.date.created | 2013-07-03 | - |
dc.date.created | 2013-07-03 | - |
dc.date.issued | 2013-04 | - |
dc.identifier.citation | NATURE COMMUNICATIONS, v.4, pp.1705 | - |
dc.identifier.issn | 2041-1723 | - |
dc.identifier.uri | http://hdl.handle.net/10203/225185 | - |
dc.description.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. | - |
dc.language | English | - |
dc.publisher | NATURE PUBLISHING GROUP | - |
dc.subject | SYNAPTIC VESICLE FUSION | - |
dc.subject | MEMBRANE-FUSION | - |
dc.subject | MAGNETIC TWEEZERS | - |
dc.subject | OPTICAL TWEEZERS | - |
dc.subject | PROTEIN MOLECULE | - |
dc.subject | SYNAPTOBREVIN | - |
dc.subject | DNA | - |
dc.subject | MICROMANIPULATION | - |
dc.subject | SYNAPTOTAGMIN-1 | - |
dc.subject | MICROSCOPY | - |
dc.title | Mechanical unzipping and rezipping of a single SNARE complex reveals hysteresis as a force-generating mechanism | - |
dc.type | Article | - |
dc.identifier.wosid | 000318872100062 | - |
dc.identifier.scopusid | 2-s2.0-84877779303 | - |
dc.type.rims | ART | - |
dc.citation.volume | 4 | - |
dc.citation.beginningpage | 1705 | - |
dc.citation.publicationname | NATURE COMMUNICATIONS | - |
dc.identifier.doi | 10.1038/ncomms2692 | - |
dc.contributor.localauthor | Cho, Yong-Hoon | - |
dc.contributor.localauthor | Yoon, Tae-Young | - |
dc.contributor.nonIdAuthor | Hyeon, Changbong | - |
dc.contributor.nonIdAuthor | Shin, Yeon-Kyun | - |
dc.description.isOpenAccess | Y | - |
dc.type.journalArticle | Article | - |
dc.subject.keywordPlus | SYNAPTIC VESICLE FUSION | - |
dc.subject.keywordPlus | MEMBRANE-FUSION | - |
dc.subject.keywordPlus | MAGNETIC TWEEZERS | - |
dc.subject.keywordPlus | OPTICAL TWEEZERS | - |
dc.subject.keywordPlus | PROTEIN MOLECULE | - |
dc.subject.keywordPlus | SYNAPTOBREVIN | - |
dc.subject.keywordPlus | DNA | - |
dc.subject.keywordPlus | MICROMANIPULATION | - |
dc.subject.keywordPlus | SYNAPTOTAGMIN-1 | - |
dc.subject.keywordPlus | MICROSCOPY | - |
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.