Syntaxin N-terminal peptide motif is an initiation factor for the assembly of the SNARE-Sec1/Munc18 membrane fusion complex
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Title
Syntaxin N-terminal peptide motif is an initiation factor for the assembly of the SNARE-Sec1/Munc18 membrane fusion complex
Authors
Keywords
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Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 107, Issue 52, Pages 22399-22406
Publisher
Proceedings of the National Academy of Sciences
Online
2010-12-08
DOI
10.1073/pnas.1012997108
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Note: Only part of the references are listed.- Single-Vesicle Fusion Assay Reveals Munc18-1 Binding to the SNARE Core Is Sufficient for Stimulating Membrane Fusion
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- Membrane Fusion: Five Lipids, Four SNAREs, Three Chaperones, Two Nucleotides, and a Rab, All Dancing in a Ring on Yeast Vacuoles
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- Binding of Munc18-1 to Synaptobrevin and to the SNARE Four-Helix Bundle
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- Protein Determinants of SNARE-Mediated Lipid Mixing
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- At the junction of SNARE and SM protein function
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- SNARE bundle and syntaxin N-peptide constitute a minimal complement for Munc18-1 activation of membrane fusion
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- Synaptobrevin N-terminally bound to syntaxin–SNAP-25 defines the primed vesicle state in regulated exocytosis
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- Mso1p Regulates Membrane Fusion through Interactions with the Putative N-Peptide–binding Area in Sec1p Domain 1
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- The SM protein Vps33 and the t-SNARE Habc domain promote fusion pore opening
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- The Functions of Munc18-1 in Regulated Exocytosis
- (2009) Robert D. Burgoyne et al. Annals of the New York Academy of Sciences
- Abrogating Munc18-1-SNARE Complex Interaction Has Limited Impact on Exocytosis in PC12 Cells
- (2009) Nancy T. Malintan et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Rescue of Munc18-1 and -2 Double Knockdown Reveals the Essential Functions of Interaction between Munc18 and Closed Syntaxin in PC12 Cells
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- Dynamic structure of lipid-bound synaptobrevin suggests a nucleation-propagation mechanism for trans-SNARE complex formation
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- Synaptic Vesicles Are Constitutively Active Fusion Machines that Function Independently of Ca 2+
- (2008) Matthew Holt et al. CURRENT BIOLOGY
- Munc18a controls SNARE assembly through its interaction with the syntaxin N-peptide
- (2008) Pawel Burkhardt et al. EMBO JOURNAL
- UNC-18 Promotes Both the Anterograde Trafficking and Synaptic Function of Syntaxin
- (2008) Jason M. McEwen et al. MOLECULAR BIOLOGY OF THE CELL
- Munc18a Scaffolds SNARE Assembly to Promote Membrane Fusion
- (2008) Travis L. Rodkey et al. MOLECULAR BIOLOGY OF THE CELL
- SNAREpin/Munc18 promotes adhesion and fusion of large vesicles to giant membranes
- (2008) D. Tareste et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Conformational Switch of Syntaxin-1 Controls Synaptic Vesicle Fusion
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