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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
2011-1-19
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pubmed:databankReference |
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pubmed:abstractText |
Munc18-1 and Syntaxin1 are essential proteins for SNARE-mediated neurotransmission. Munc18-1 participates in synaptic vesicle fusion via dual roles: as a docking/chaperone protein by binding closed Syntaxin1, and as a fusion protein that binds SNARE complexes in a Syntaxin1 N-peptide dependent manner. The two roles are associated with a closed-open Syntaxin1 conformational transition. Here, we show that Syntaxin N-peptide binding to Munc18-1 is not highly selective, suggesting that other parts of the SNARE complex are involved in binding to Munc18-1. We also find that Syntaxin1, with an N peptide and a physically anchored C terminus, binds to Munc18-1 and that this complex can participate in SNARE complex formation. We report a Munc18-1-N-peptide crystal structure that, together with other data, reveals how Munc18-1 might transit from a conformation that binds closed Syntaxin1 to one that may be compatible with binding open Syntaxin1 and SNARE complexes. Our results suggest the possibility that structural transitions occur in both Munc18-1 and Syntaxin1 during their binary interaction. We hypothesize that Munc18-1 domain 3a undergoes a conformational change that may allow coiled-coil interactions with SNARE complexes.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/21193638-10336434,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/21193638-9045631
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
1091-6490
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
18
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pubmed:volume |
108
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1040-5
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pubmed:dateRevised |
2011-8-1
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pubmed:meshHeading |
pubmed-meshheading:21193638-Amino Acid Sequence,
pubmed-meshheading:21193638-Circular Dichroism,
pubmed-meshheading:21193638-Crystallography,
pubmed-meshheading:21193638-Models, Molecular,
pubmed-meshheading:21193638-Molecular Sequence Data,
pubmed-meshheading:21193638-Multiprotein Complexes,
pubmed-meshheading:21193638-Munc18 Proteins,
pubmed-meshheading:21193638-Protein Binding,
pubmed-meshheading:21193638-Protein Conformation,
pubmed-meshheading:21193638-SNARE Proteins,
pubmed-meshheading:21193638-Sequence Alignment,
pubmed-meshheading:21193638-Synaptic Transmission,
pubmed-meshheading:21193638-Syntaxin 1
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pubmed:year |
2011
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pubmed:articleTitle |
Possible roles for Munc18-1 domain 3a and Syntaxin1 N-peptide and C-terminal anchor in SNARE complex formation.
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pubmed:affiliation |
Institute for Molecular Bioscience, Division of Chemistry and Structural Biology, The University of Queensland, Brisbane, Queensland 4072, Australia.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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