Full metadata record
DC Field | Value | Language |
---|---|---|
dc.citation.startPage | 8700 | - |
dc.citation.title | SCIENTIFIC REPORTS | - |
dc.citation.volume | 7 | - |
dc.contributor.author | Kim, Kyung Tae | - |
dc.contributor.author | Moon, Yeojin | - |
dc.contributor.author | Jang, Yunsu | - |
dc.contributor.author | Lee, Kang Taek | - |
dc.contributor.author | Lee, Changwook | - |
dc.contributor.author | Jun, Youngsoo | - |
dc.contributor.author | Lee, Sanghwa | - |
dc.date.accessioned | 2023-12-21T22:06:25Z | - |
dc.date.available | 2023-12-21T22:06:25Z | - |
dc.date.created | 2017-08-29 | - |
dc.date.issued | 2017-08 | - |
dc.description.abstract | Homotypic fusion of endoplasmic reticulum membranes is driven by atlastin GTPases; however, the underlying mechanism remains largely unknown. Here, using a FRET-based single-vesicle fusion assay with liposomes bearing the yeast atlastin Sey1p, we investigated the molecular mechanisms of atlastin-mediated membrane tethering and fusion. Although Sey1p-bearing proteoliposomes frequently underwent membrane tethering in a GTP hydrolysis-dependent manner as reported in studies using bulk assays, only a small fraction of the tethered liposomes proceeded to fusion. Strikingly, the rest of the tethered liposomes failed to fuse or dissociate. This stable tethering, however, did not require continued GTP hydrolysis because GTP omission and magnesium chelation did not disrupt tethering. Interestingly, an increased Sey1p density on the membrane markedly accelerated tethering but barely affected the fusion rate of the tethered liposomes, indicating that Sey1p requires additional factors to support efficient fusion in vivo. Finally, the assay also revealed that Sey1p-mediated liposome fusion occurs through hemifusion, suggesting the mechanistic conservation between biological membrane fusion events despite the existence of diverse fusogens. | - |
dc.identifier.bibliographicCitation | SCIENTIFIC REPORTS, v.7, pp.8700 | - |
dc.identifier.doi | 10.1038/s41598-017-09162-9 | - |
dc.identifier.issn | 2045-2322 | - |
dc.identifier.scopusid | 2-s2.0-85027727968 | - |
dc.identifier.uri | https://scholarworks.unist.ac.kr/handle/201301/22602 | - |
dc.identifier.url | https://www.nature.com/articles/s41598-017-09162-9 | - |
dc.identifier.wosid | 000407979900012 | - |
dc.language | 영어 | - |
dc.publisher | NATURE PUBLISHING GROUP | - |
dc.title | Molecular mechanisms of atlastin-mediated ER membrane fusion revealed by a FRET-based single-vesicle fusion assay | - |
dc.type | Article | - |
dc.description.isOpenAccess | TRUE | - |
dc.relation.journalWebOfScienceCategory | Multidisciplinary Sciences | - |
dc.relation.journalResearchArea | Science & Technology - Other Topics | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.subject.keywordPlus | ENDOPLASMIC-RETICULUM | - |
dc.subject.keywordPlus | HOMOTYPIC FUSION | - |
dc.subject.keywordPlus | STRUCTURAL BASIS | - |
dc.subject.keywordPlus | PROVIDE INSIGHT | - |
dc.subject.keywordPlus | CEREVISIAE | - |
dc.subject.keywordPlus | COMPLEXES | - |
dc.subject.keywordPlus | NETWORK | - |
dc.subject.keywordPlus | GTPASES | - |
dc.subject.keywordPlus | SNARES | - |
Items in Repository are protected by copyright, with all rights reserved, unless otherwise indicated.
Tel : 052-217-1404 / Email : scholarworks@unist.ac.kr
Copyright (c) 2023 by UNIST LIBRARY. All rights reserved.
ScholarWorks@UNIST was established as an OAK Project for the National Library of Korea.