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New component of the vacuolar class C-Vps complex couples nucleotide exchange on the Ypt7 GTPase to SNARE-dependent docking and fusion
scientific article
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scholarly article
1 reference
stated in
PubMed
PubMed ID
11062257
retrieved
1 December 2016
title
New component of the vacuolar class C-Vps complex couples nucleotide exchange on the Ypt7 GTPase to SNARE-dependent docking and fusion
(English)
1 reference
stated in
PubMed
PubMed ID
11062257
retrieved
1 December 2016
main subject
Vam6p YDL077C
1 reference
stated in
GOA release 2020-03-11
Rab family GTPase YPT7 YML001W
1 reference
stated in
GOA release 2020-03-11
author name string
T K Sato
series ordinal
2
0 references
S D Emr
series ordinal
3
0 references
A E Wurmser
series ordinal
1
0 references
language of work or name
English
0 references
publication date
30 October 2000
0 references
published in
Journal of Cell Biology
1 reference
stated in
PubMed
PubMed ID
11062257
retrieved
1 December 2016
volume
151
0 references
issue
3
0 references
page(s)
551-62
0 references
cites work
Class C Vps protein complex regulates vacuolar SNARE pairing and is required for vesicle docking/fusion
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PubMed Central
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A Ypt/Rab effector complex containing the Sec1 homolog Vps33p is required for homotypic vacuole fusion
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Formation of AP-3 transport intermediates requires Vps41 function
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The Rab5 effector EEA1 interacts directly with syntaxin-6
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Clathrin self-assembly is mediated by a tandemly repeated superhelix
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The exocyst is an effector for Sec4p, targeting secretory vesicles to sites of exocytosis
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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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TRAPP, a highly conserved novel complex on the cis-Golgi that mediates vesicle docking and fusion
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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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A multispecificity syntaxin homologue, Vam3p, essential for autophagic and biosynthetic protein transport to the vacuole
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PubMed Central
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Vam3p, a new member of syntaxin related protein, is required for vacuolar assembly in the yeast Saccharomyces cerevisiae
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PubMed Central
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20 March 2017
Sec2p mediates nucleotide exchange on Sec4p and is involved in polarized delivery of post-Golgi vesicles
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Novel Golgi to vacuole delivery pathway in yeast: identification of a sorting determinant and required transport component.
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Endosomal transport function in yeast requires a novel AAA-type ATPase, Vps4p
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Vam2/Vps41p and Vam6/Vps39p are components of a protein complex on the vacuolar membranes and involved in the vacuolar assembly in the yeast Saccharomyces cerevisiae
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The Exocyst is a multiprotein complex required for exocytosis in Saccharomyces cerevisiae
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Rabaptin-5 is a direct effector of the small GTPase Rab5 in endocytic membrane fusion
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Role of three rab5-like GTPases, Ypt51p, Ypt52p, and Ypt53p, in the endocytic and vacuolar protein sorting pathways of yeast
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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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20 March 2017
Protein sorting in Saccharomyces cerevisiae: isolation of mutants defective in the delivery and processing of multiple vacuolar hydrolases
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20 March 2017
The fungal vacuole: composition, function, and biogenesis
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20 March 2017
Morphological classification of the yeast vacuolar protein sorting mutants: evidence for a prevacuolar compartment in class E vps mutants
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20 March 2017
Endocytosis in yeast: evidence for the involvement of a small GTP-binding protein (Ypt7p)
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20 March 2017
Aminopeptidase I of Saccharomyces cerevisiae is localized to the vacuole independent of the secretory pathway
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20 March 2017
Oligomeric complexes link Rab5 effectors with NSF and drive membrane fusion via interactions between EEA1 and syntaxin 13
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A novel Rab5 GDP/GTP exchange factor complexed to Rabaptin-5 links nucleotide exchange to effector recruitment and function
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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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Vam7p, a SNAP-25-like molecule, and Vam3p, a syntaxin homolog, function together in yeast vacuolar protein trafficking
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29 September 2017
A novel Sec18p/NSF-dependent complex required for Golgi-to-endosome transport in yeast
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Yeast vacuolar proenzymes are sorted in the late Golgi complex and transported to the vacuole via a prevacuolar endosome-like compartment
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29 September 2017
VPS21 encodes a rab5-like GTP binding protein that is required for the sorting of yeast vacuolar proteins.
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29 September 2017
Mutational analysis of the putative effector domain of the GTP-binding Ypt1 protein in yeast suggests specific regulation by a novel GAP activity
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A putative zinc finger protein, Saccharomyces cerevisiae Vps18p, affects late Golgi functions required for vacuolar protein sorting and efficient alpha-factor prohormone maturation
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29 September 2017
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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2 June 2018
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2 June 2018
Genes for directing vacuolar morphogenesis in Saccharomyces cerevisiae. II. VAM7, a gene for regulating morphogenic assembly of the vacuoles
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2 June 2018
A role for the deep orange and carnation eye color genes in lysosomal delivery in Drosophila
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21 January 2018
Defining the functions of trans-SNARE pairs
1 reference
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Crossref
reference URL
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21 January 2018
Evidence for a symmetrical requirement for Rab5-GTP in in vitro endosome-endosome fusion
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/11062257
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Genes for directing vacuolar morphogenesis in Saccharomyces cerevisiae. I. Isolation and characterization of two classes of vam mutants
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/11062257
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Elongation factor Tu D138N, a mutant with modified substrate specificity, as a tool to study energy consumption in protein biosynthesis
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/11062257
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Identifiers
DOI
10.1083/JCB.151.3.551
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
1101546
Fatcat ID
release_nqeomm6pxbghnd2lkvsftr2wte
1 reference
stated in
Fatcat
reference URL
https://api.fatcat.wiki/v0/release/nqeomm6pxbghnd2lkvsftr2wte
retrieved
24 November 2022
based on heuristic
mapped directly with Wikidata item
OpenCitations bibliographic resource ID
1101546
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
1101546
PMCID
2185595
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
1101546
PubMed ID
11062257
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
1101546
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