Reconciling the regulatory role of Munc18 proteins in SNARE-complex assembly

Rehman, Asma, Archbold, Julia, Hu, Shu-Hong, Norwood, Suzanne, Collins, Brett and Martin, Jennifer L. (2014) Reconciling the regulatory role of Munc18 proteins in SNARE-complex assembly. IUCrJ, 1 6: 505-513. doi:10.1107/S2052252514020727

Author Rehman, Asma
Archbold, Julia
Hu, Shu-Hong
Norwood, Suzanne
Collins, Brett
Martin, Jennifer L.
Title Reconciling the regulatory role of Munc18 proteins in SNARE-complex assembly
Journal name IUCrJ   Check publisher's open access policy
ISSN 2052-2525
Publication date 2014-10
Year available 2014
Sub-type Article (original research)
DOI 10.1107/S2052252514020727
Open Access Status DOI
Volume 1
Issue 6
Start page 505
End page 513
Total pages 9
Place of publication Chester, United Kingdom
Publisher International Union of Crystallography
Collection year 2015
Language eng
Formatted abstract
Membrane fusion is essential for human health, playing a vital role in processes as diverse as neurotransmission and blood glucose control. Two protein families are key: (1) the Sec1p/Munc18 (SM) and (2) the soluble N-ethylmaleimide-sensitive attachment protein receptor (SNARE) proteins. Whilst the essential nature of these proteins is irrefutable, their exact regulatory roles in membrane fusion remain controversial. In particular, whether SM proteins promote and/or inhibit the SNARE-complex formation required for membrane fusion is not resolved. Crystal structures of SM proteins alone and in complex with their cognate SNARE proteins have provided some insight, however, these structures lack the transmembrane spanning regions of the SNARE proteins and may not accurately reflect the native state. Here, we review the literature surrounding the regulatory role of mammalian Munc18 SM proteins required for exocytosis in eukaryotes. Our analysis suggests that the conflicting roles reported for these SM proteins may reflect differences in experimental design. SNARE proteins appear to require C-terminal immobilization or anchoring, for example through a transmembrane domain, to form a functional fusion complex in the presence of Munc18 proteins.
Keyword Sm Proteins
Snare Proteins
Membrane Trafficking
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: Official 2015 Collection
Institute for Molecular Bioscience - Publications
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Created: Wed, 07 Jan 2015, 11:55:51 EST by Susan Allen on behalf of Institute for Molecular Bioscience