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Lee, Changwook
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dc.citation.number 4 -
dc.citation.startPage e202109090 -
dc.citation.title JOURNAL OF CELL BIOLOGY -
dc.citation.volume 222 -
dc.contributor.author Jang, Eunhong -
dc.contributor.author Moon, Yeojin -
dc.contributor.author Yoon, So Young -
dc.contributor.author Diaz, Joyce Anne R. -
dc.contributor.author Lee, Miriam -
dc.contributor.author Ko, Naho -
dc.contributor.author Park, Jongseo -
dc.contributor.author Eom, Soo Hyun -
dc.contributor.author Lee, Changwook -
dc.contributor.author Jun, Youngsoo -
dc.date.accessioned 2023-12-21T13:06:33Z -
dc.date.available 2023-12-21T13:06:33Z -
dc.date.created 2023-05-17 -
dc.date.issued 2023-02 -
dc.description.abstract The dynamin-like GTPase atlastin is believed to be the minimal machinery required for homotypic endoplasmic reticulum (ER) membrane fusion, mainly because Drosophila atlastin is sufficient to drive liposome fusion. However, it remains unclear whether mammalian atlastins, including the three human atlastins, are sufficient to induce liposome fusion, raising doubts about their major roles in mammalian cells. Here, we show that all human atlastins are sufficient to induce fusion when reconstituted into liposomes with a lipid composition mimicking that of the ER. Although the fusogenic activity of ATL1, which is predominantly expressed in neuronal cells, was weaker than that of ATL2 or ATL3, the addition of M1-spastin, a neuron-specific factor, markedly increased ATL1-mediated liposome fusion. Although we observed efficient fusion between ER microsomes isolated from cultured, non-neuronal cells that predominantly express ATL2-1, an autoinhibited isoform of ATL2, ATL2-1 failed to support liposome fusion by itself as reported previously, indicating that cellular factors enable ATL2-1 to mediate ER fusion in vivo. Atlastins regulate the structure and function of the endoplasmic reticulum (ER). In this study, using reconstituted proteoliposomes with a lipid composition mimicking that of the ER, Jang et al. show that all human atlastins are sufficient to drive membrane fusion. -
dc.identifier.bibliographicCitation JOURNAL OF CELL BIOLOGY, v.222, no.4, pp.e202109090 -
dc.identifier.doi 10.1083/jcb.202109090 -
dc.identifier.issn 0021-9525 -
dc.identifier.scopusid 2-s2.0-85147834173 -
dc.identifier.uri https://scholarworks.unist.ac.kr/handle/201301/64337 -
dc.identifier.url http://dx.doi.org/10.1083/jcb.202109090 -
dc.identifier.wosid 000978274100001 -
dc.language 영어 -
dc.publisher ROCKEFELLER UNIV PRESS -
dc.title Human atlastins are sufficient to drive the fusion of liposomes with a physiological lipid composition -
dc.type Article -
dc.description.isOpenAccess FALSE -
dc.relation.journalWebOfScienceCategory Cell Biology -
dc.relation.journalResearchArea Cell Biology -
dc.type.docType Article -
dc.description.journalRegisteredClass scie -
dc.description.journalRegisteredClass scopus -
dc.subject.keywordPlus HEREDITARY SPASTIC PARAPLEGIA -
dc.subject.keywordPlus HOMOTYPIC ER FUSION -
dc.subject.keywordPlus VERTEX RING DOMAIN -
dc.subject.keywordPlus GOLGI-APPARATUS -
dc.subject.keywordPlus MEMBRANE -
dc.subject.keywordPlus PROTEINS -
dc.subject.keywordPlus GTPASES -
dc.subject.keywordPlus SNARES -
dc.subject.keywordPlus ASSOCIATION -
dc.subject.keywordPlus PATHWAY -

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