Class C Vps protein complex regulates vacuolar SNARE pairing and is required for vesicle docking/fusion (Q27940206)

PubMed

1 December 2016

title

Class C Vps protein complex regulates vacuolar SNARE pairing and is required for vesicle docking/fusion (English)

1 reference

PubMed

Tethering complex subunit PEP3 YLR148W

1 December 2016

main subject

1 reference

GOA release 2020-03-11

author name string

T K Sato

1

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P Rehling

2

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M R Peterson

3

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S D Emr

4

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publication date

September 2000

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language of work or name

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1 reference

A novel Sec18p/NSF-dependent complex required for Golgi-to-endosome transport in yeast

1 December 2016

volume

6

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issue

3

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page(s)

661-71

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cites work

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A multispecificity syntaxin homologue, Vam3p, essential for autophagic and biosynthetic protein transport to the vacuole

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The yeast v-SNARE Vti1p mediates two vesicle transport pathways through interactions with the t-SNAREs Sed5p and Pep12p

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The Saccharomyces cerevisiae v-SNARE Vti1p is required for multiple membrane transport pathways to the vacuole

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Tomosyn: a Syntaxin-1–Binding Protein that Forms a Novel Complex in the Neurotransmitter Release Process

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A new beat for the SNARE drum

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The exocyst is an effector for Sec4p, targeting secretory vesicles to sites of exocytosis

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The GTPase Ypt7p of Saccharomyces cerevisiae is required on both partner vacuoles for the homotypic fusion step of vacuole inheritance.

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The Sec1 family: a novel family of proteins involved in synaptic transmission and general secretion.

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Synaptic vesicle fusion complex contains unc-18 homologue bound to syntaxin

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Membrane fusion and exocytosis

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Syntaphilin: a syntaxin-1 clamp that controls SNARE assembly

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Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae

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Sec18p (NSF)-driven release of Sec17p (alpha-SNAP) can precede docking and fusion of yeast vacuoles

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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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Intracellular membrane fusion: SNAREs only?

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Oligomeric complexes link Rab5 effectors with NSF and drive membrane fusion via interactions between EEA1 and syntaxin 13

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Complexins: cytosolic proteins that regulate SNAP receptor function

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Homotypic vacuolar fusion mediated by t- and v-SNAREs

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The diversity of Rab proteins in vesicle transport

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Vac1p coordinates Rab and phosphatidylinositol 3-kinase signaling in Vps45p-dependent vesicle docking/fusion at the endosome

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Transport vesicle docking: SNAREs and associates

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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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Proteins needed for vesicle budding from the Golgi complex are also required for the docking step of homotypic vacuole fusion

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7 January 2021

Formation of AP-3 transport intermediates requires Vps41 function

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A Novel RING Finger Protein Complex Essential for a Late Step in Protein Transport to the Yeast Vacuole

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TRAPP, a highly conserved novel complex on the cis-Golgi that mediates vesicle docking and fusion

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Vam7p, a SNAP-25-Like Molecule, and Vam3p, a Syntaxin Homolog, Function Together in Yeast Vacuolar Protein Trafficking

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Vam7p, a vacuolar SNAP-25 homolog, is required for SNARE complex integrity and vacuole docking and fusion

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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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7 January 2021

Three v-SNAREs and two t-SNAREs, present in a pentameric cis-SNARE complex on isolated vacuoles, are essential for homotypic fusion.

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ROP, the Drosophila Sec1 homolog, interacts with syntaxin and regulates neurotransmitter release in a dosage-dependent manner.

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Phosphoinositide signaling and turnover: PtdIns(3)P, a regulator of membrane traffic, is transported to the vacuole and degraded by a process that requires lumenal vacuolar hydrolase activities

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nSec1 binds a closed conformation of syntaxin1A.

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Identifiers

DOI

1 reference

Consolidated OpenCitations Corpus – April 2017

1 reference

Consolidated OpenCitations Corpus – April 2017

1 reference

Consolidated OpenCitations Corpus – April 2017