A direct role for the Sec1/Munc18-family protein Vps33 as a template for SNARE assembly
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Title
A direct role for the Sec1/Munc18-family protein Vps33 as a template for SNARE assembly
Authors
Keywords
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Journal
SCIENCE
Volume 349, Issue 6252, Pages 1111-1114
Publisher
American Association for the Advancement of Science (AAAS)
Online
2015-09-04
DOI
10.1126/science.aac7906
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Note: Only part of the references are listed.- An Extended Helical Conformation in Domain 3a of Munc18-1 Provides a Template for SNARE (SolubleN-Ethylmaleimide-sensitive Factor Attachment Protein Receptor) Complex Assembly
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- The tethering complex HOPS catalyzes assembly of the soluble SNARE Vam7 into fusogenic trans-SNARE complexes
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- Crystal Structures of the Sec1/Munc18 (SM) Protein Vps33, Alone and Bound to the Homotypic Fusion and Vacuolar Protein Sorting (HOPS) Subunit Vps16*
- (2013) Richard W. Baker et al. PLoS One
- Structural basis of Vps33A recruitment to the human HOPS complex by Vps16
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- The Membrane Fusion Enigma: SNAREs, Sec1/Munc18 Proteins, and Their Accomplices—Guilty as Charged?
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- Sec1/Munc18 protein Vps33 binds to SNARE domains and the quaternary SNARE complex
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- Reconstitution of the Vital Functions of Munc18 and Munc13 in Neurotransmitter Release
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- Data processing and analysis with theautoPROCtoolbox
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- HOPS drives vacuole fusion by binding the vacuolar SNARE complex and the Vam7 PX domain via two distinct sites
- (2011) Lukas Krämer et al. MOLECULAR BIOLOGY OF THE CELL
- Membrane fusion catalyzed by a Rab, SNAREs, and SNARE chaperones is accompanied by enhanced permeability to small molecules and by lysis
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- Primordial neurosecretory apparatus identified in the choanoflagellate Monosiga brevicollis
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- Tethering Factors as Organizers of Intracellular Vesicular Traffic
- (2010) I-Mei Yu et al. Annual Review of Cell and Developmental Biology
- Membrane Fusion: Five Lipids, Four SNAREs, Three Chaperones, Two Nucleotides, and a Rab, All Dancing in a Ring on Yeast Vacuoles
- (2010) William Wickner Annual Review of Cell and Developmental Biology
- Binding of Munc18-1 to Synaptobrevin and to the SNARE Four-Helix Bundle
- (2010) Yi Xu et al. BIOCHEMISTRY
- HOPS prevents the disassembly of trans-SNARE complexes by Sec17p/Sec18p during membrane fusion
- (2010) Hao Xu et al. EMBO JOURNAL
- ConSurf 2010: calculating evolutionary conservation in sequence and structure of proteins and nucleic acids
- (2010) H. Ashkenazy et al. NUCLEIC ACIDS RESEARCH
- Possible roles for Munc18-1 domain 3a and Syntaxin1 N-peptide and C-terminal anchor in SNARE complex formation
- (2010) S.-H. Hu et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Capture and release of partially zipped trans-SNARE complexes on intact organelles
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- Reconstituted membrane fusion requires regulatory lipids, SNAREs and synergistic SNARE chaperones
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- Munc18a controls SNARE assembly through its interaction with the syntaxin N-peptide
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- HOPS Proofreads the trans-SNARE Complex for Yeast Vacuole Fusion
- (2008) Vincent J. Starai et al. MOLECULAR BIOLOGY OF THE CELL
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