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dc.contributor.authorCollins, BM
dc.contributor.authorMartin, JL
dc.date.accessioned2018-01-24T01:51:58Z
dc.date.available2018-01-24T01:51:58Z
dc.date.issued2015
dc.identifier.issn1545-9993
dc.identifier.doi10.1038/nsmb.3094
dc.identifier.urihttp://hdl.handle.net/10072/123558
dc.description.abstractMembrane fusion is a fundamentally important process that supports delivery of cellular cargo in systems as diverse as neurotransmission, blood glucose control and mast-cell degranulation. The 2013 Nobel Prize in Physiology or Medicine, awarded to Rothman, Schekman and Südhof1, celebrated their discoveries of the essential membrane-fusion machinery, comprising the SNARE and the Sec1–Munc18 (SM) protein families (Fig. 1). Cognate SNARE partners act as molecular zippers that bring apposing membranes together, but the precise molecular role of the SM proteins has proven much more elusive. A recent article by Baker et al. in Science2 provides new insights into how this vital component operates.
dc.languageEnglish
dc.language.isoeng
dc.publisherNature Publishing Group
dc.relation.ispartofpagefrom756
dc.relation.ispartofpageto758
dc.relation.ispartofissue10
dc.relation.ispartofjournalNature Structural and Molecular Biology
dc.relation.ispartofvolume22
dc.subject.fieldofresearchChemical sciences
dc.subject.fieldofresearchBiological sciences
dc.subject.fieldofresearchOther biological sciences not elsewhere classified
dc.subject.fieldofresearchBiomedical and clinical sciences
dc.subject.fieldofresearchcode34
dc.subject.fieldofresearchcode31
dc.subject.fieldofresearchcode319999
dc.subject.fieldofresearchcode32
dc.titleSEC-uring membrane fusion: a sneak peek at SNARE-complex assembly driven by Sec1-Munc18 proteins
dc.typeJournal article
dc.type.descriptionC2 - Articles (Other)
dc.type.codeC - Journal Articles
gro.hasfulltextNo Full Text
gro.griffith.authorMartin, Jennifer


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