The V‐ATPase proteolipid cylinder promotes the lipid‐mixing stage of SNARE‐dependent fusion of yeast vacuoles

No abstract is available for this paper.

• Publication year

  2011

• Venue

  EMBO Journal

• Publication date

  2011-10-19

• Fields of study

  Biology, Medicine

• Identifiers
  DOI 10.1038/emboj.2011.335PMID 21934648PMCID PMC3199395
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

• A role for V‐ATPase subunits in synaptic vesicle fusion?

  2011cited by this paper
• HOPS prevents the disassembly of trans‐SNARE complexes by Sec17p/Sec18p during membrane fusion

  2010cited by this paper
• A dual function of V0-ATPase a1 provides an endolysosomal degradation mechanism in Drosophila melanogaster photoreceptors

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• The SM protein Vps33 and the t-SNARE Habc domain promote fusion pore opening

  2010cited by this paper
• Experimental evidence for membrane-mediated protein-protein interaction.

  2010cited by this paper
• Membrane curvature in synaptic vesicle fusion and beyond.

  2010cited by this paper
• V-ATPase membrane sector associates with synaptobrevin to modulate neurotransmitter release.

  2010cited by this paper
• HOPS Initiates Vacuole Docking by Tethering Membranes before trans-SNARE Complex Assembly

  2010cited by this paper
• Progress in understanding the neuronal SNARE function and its regulation

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  2009cited by this paper
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  2008cited by this paper
• Mechanics of membrane fusion

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  2008cited by this paper
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  2008cited by this paper
• Structure of the Yeast Vacuolar ATPase*

  2008cited by this paper
• The vacuolar V1/V0‐ATPase is involved in the release of the HOPS subunit Vps41 from vacuoles, vacuole fragmentation and fusion

  2008cited by this paper
• The fusion pores of Ca2+-triggered exocytosis

  2008cited by this paper
• Reconstituted membrane fusion requires regulatory lipids, SNAREs and synergistic SNARE chaperones

  2008cited by this paper
• Role of the V-ATPase in regulation of the vacuolar fission-fusion equilibrium.

  2007cited by this paper
• trans-SNARE complex assembly and yeast vacuole membrane fusion

  2007cited by this paper
• Arrangement of Subunits in the Proteolipid Ring of the V-ATPase*

  2007cited by this paper
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  2007cited by this paper
• The role of transmembrane domains in membrane fusion

  2007cited by this paper
• Unraveling the mechanisms of synaptotagmin and SNARE function in neurotransmitter release.

  2006cited by this paper
• The a3 isoform of V-ATPase regulates insulin secretion from pancreatic beta-cells.

  2006cited by this paper
• The V0-ATPase mediates apical secretion of exosomes containing Hedgehog-related proteins in Caenorhabditis elegans

  2006cited by this paper
• Membranes of the world unite!

  2006cited by this paper
• Sequential N‐ to C‐terminal SNARE complex assembly drives priming and fusion of secretory vesicles

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  2006cited by this paper
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  2006cited by this paper
• The a3 isoform of V-ATPase regulates insulin secretion from pancreatic β-cells

  2006cited by this paper
• A Model for the Proteolipid Ring and Bafilomycin/Concanamycin-binding Site in the Vacuolar ATPase of Neurospora crassa*

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• A Partially Zipped SNARE Complex Stabilized by the Membrane*

  2005cited by this paper
• The vacuolar kinase Yck3 maintains organelle fragmentation by regulating the HOPS tethering complex

  2005cited by this paper
• Trans-SNARE pairing can precede a hemifusion intermediate in intracellular membrane fusion

  2005cited by this paper
• The v-ATPase V0 subunit a1 is required for a late step in synaptic vesicle exocytosis in Drosophila.

  2005cited by this paper
• Sec17p and HOPS, in distinct SNARE complexes, mediate SNARE complex disruption or assembly for fusion

  2005cited by this paper
• Transition from hemifusion to pore opening is rate limiting for vacuole membrane fusion

  2005cited by this paper
• Structure of the Rotor of the V-Type Na+-ATPase from Enterococcus hirae

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• Topological Characterization of the c, c′, and c″ Subunits of the Vacuolar ATPase from the Yeast Saccharomyces cerevisiae*

  2004cited by this paper
• The Bafilomycin/Concanamycin Binding Site in Subunit c of the V-ATPases from Neurospora crassa and Saccharomyces cerevisiae*

  2004cited by this paper
• Transmembrane Segments of Syntaxin Line the Fusion Pore of Ca2+-Triggered Exocytosis

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• A soluble SNARE drives rapid docking, bypassing ATP and Sec17/18p for vacuole fusion

  2004cited by this paper
• Control of eukaryotic membrane fusion by N-terminal domains of SNARE proteins.

  2003cited by this paper
• The First Putative Transmembrane Segment of Subunit c" (Vma16p) of the Yeast V-ATPase Is Not Necessary for Function*

  2003cited by this paper
• Vacuole membrane fusion: V 0 functions after trans-SNARE pairing and is coupled to the Ca 2 (cid:2) -releasing channel

  2003cited by this paper
• Specific sorting of the a1 isoform of the V-H+ATPase a subunit to nerve terminals where it associates with both synaptic vesicles and the presynaptic plasma membrane

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• Structure and Assembly of the Yeast V-ATPase

  2003cited by this paper
• Vacuole membrane fusion

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• The RAVE Complex Is Essential for Stable Assembly of the Yeast V-ATPase*

  2002cited by this paper
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• Microtubules Are Involved in Glucose-dependent Dissociation of the Yeast Vacuolar [H+]-ATPase in Vivo *

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• Trans-complex formation by proteolipid channels in the terminal phase of membrane fusion

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• Fusion needs more than SNAREs

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• Neurotransmitter release through the V0 sector of V‐ATPase

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• Close Is Not Enough

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• The Docking Stage of Yeast Vacuole Fusion Requires the Transfer of Proteins from a Cis-Snare Complex to a Rab/Ypt Protein

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• Class C Vps protein complex regulates vacuolar SNARE pairing and is required for vesicle docking/fusion.

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• Molecular Characterization of the Yeast Vacuolar H+-ATPase Proton Pore*

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• A Vacuolar v–t-SNARE Complex, the Predominant Form In Vivo and on Isolated Vacuoles, Is Disassembled and Activated for Docking and Fusion

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• VMA11 and VMA16 Encode Second and Third Proteolipid Subunits of the Saccharomyces cerevisiae Vacuolar Membrane H+-ATPase*

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• Docking of Yeast Vacuoles Is Catalyzed by the Ras-like GTPase Ypt7p after Symmetric Priming by Sec18p (NSF)

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• The V Sector of the V-ATPase, Synaptobrevin, and Synaptophysin Are Associated on Synaptic Vesicles in a Triton X-100-resistant, Freeze-thawing Sensitive, Complex (*)

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  2025cites this paper
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