| Characterization of two distinct binding modes between syntaxin 4 and Munc18c. | |
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MedLine Citation:
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PMID: 19193195 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Interaction of SM (Sec1/Munc18) proteins with their cognate syntaxins represents an important regulatory mechanism of SNARE (soluble N-ethylmaleimide-sensitive fusion protein-attachment protein receptor)-mediated membrane fusion. Understanding the conserved mechanisms by which SM proteins function in this process has proved challenging, largely due to an apparent lack of conservation of binding mechanisms between different SM-syntaxin pairs. In the present study, we have identified a hitherto uncharacterized mode of binding between syntaxin 4 and Munc18c that is independent of the binding mode shown previously to utilize the N-terminal peptide of syntaxin 4. Our data demonstrate that syntaxin 4 and Munc18c interact via two distinct modes of binding, analogous to those employed by syntaxin 1a-Munc18a and syntaxin 16-Vps45p (vacuolar protein sorting 45). These data support the notion that all syntaxin/SM proteins bind using conserved mechanisms, and pave the way for the formulation of unifying hypotheses of SM protein function. |
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Authors:
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Veronica Aran; Fiona M Brandie; Alasdair R Boyd; Theodoros Kantidakis; Elizabeth J Rideout; Sharon M Kelly; Gwyn W Gould; Nia J Bryant |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: The Biochemical journal Volume: 419 ISSN: 1470-8728 ISO Abbreviation: Biochem. J. Publication Date: 2009 May |
Date Detail:
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Created Date: 2009-04-09 Completed Date: 2009-04-21 Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 2984726R Medline TA: Biochem J Country: England |
Other Details:
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Languages: eng Pagination: 655-60 Citation Subset: IM |
Affiliation:
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Henry Wellcome Laboratory of Cell Biology, Division of Molecular and Cellular Biology, Davidson Building, Faculty of Biomedical and Life Science, University of Glasgow, Glasgow, U.K. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Animals Munc18 Proteins / metabolism* Mutant Proteins / metabolism Peptide Hydrolases / metabolism Protein Binding Qa-SNARE Proteins / metabolism* Recombinant Fusion Proteins / metabolism |
| Grant Support | |
ID/Acronym/Agency:
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B19375//Biotechnology and Biological Sciences Research Council; BB/D000211/1//Biotechnology and Biological Sciences Research Council |
| Chemical | |
Reg. No./Substance:
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0/Munc18 Proteins; 0/Mutant Proteins; 0/Qa-SNARE Proteins; 0/Recombinant Fusion Proteins; EC 3.4.-/Peptide Hydrolases |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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