Autoinhibition of SNARE complex assembly by a conformational switch represents a conserved feature of syntaxins

MacDonald, C., Munson, M. and Bryant, N.J. (2010) Autoinhibition of SNARE complex assembly by a conformational switch represents a conserved feature of syntaxins. Biochemical Society Transactions, 38(1), pp. 209-212. (doi: 10.1042/BST0380209) (PMID:20074061) (PMCID:PMC5242387)

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Regulation and specificity of membrane trafficking are required to maintain organelle integrity while performing essential cellular transport. Membrane fusion events in all eukaryotic cells are facilitated by the formation of specific SNARE (soluble N-ethylmaleimide-sensitive fusion proteinattachment protein receptor) complexes between proteins on opposing lipid bilayers. Although regulation of SNARE complex assembly is not well understood, it is clear that two conserved protein families, the Sx (syntaxin) and the SM (Sec1p/Munc18) proteins, are central to this process. Sxs are a subfamily of SNARE proteins; in addition to the coiled-coil SNARE motif, Sxs possess an N-terminal, autonomously folded, triple-helical (Habc) domain. For some Sxs, it has been demonstrated that this Habc domain exerts an autoinhibitory effect on SNARE complex assembly by making intramolecular contacts with the SNARE motif. SM proteins regulate membrane fusion through interactions with their cognate Sxs. One hypothesis for SM protein function is that they facilitate a switch of the Sx from a closed to an open conformation, thus lifting the inhibitory action of the Habc domain and freeing the SNARE motif to participate in SNARE complexes. However, whether these regulatory mechanisms are conserved throughout the Sx/SM protein families remains contentious as it is not clear whether the closed conformation represents a universal feature of Sxs.

Item Type:Articles
Glasgow Author(s) Enlighten ID:MacDonald, Mr Chris and Bryant, Dr Nia
Authors: MacDonald, C., Munson, M., and Bryant, N.J.
Subjects:Q Science > QH Natural history > QH345 Biochemistry
College/School:College of Medical Veterinary and Life Sciences > Institute of Molecular Cell and Systems Biology
Journal Name:Biochemical Society Transactions
ISSN (Online):1470-8752

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Project CodeAward NoProject NamePrincipal InvestigatorFunder's NameFunder RefLead Dept
451371Role of the Sec1p/Munc18 (SM) protein Vps45p in SNARE complex assembly and bilayer fusionNia BryantBiotechnology and Biological Sciences Research Council (BBSRC)BB/E024904/1Institute of Molecular Cell and Systems Biology