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The CORVET subunit Vps8 cooperates with the Rab5 homolog Vps21 to induce clustering of late endosomal compartments
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scholarly article
1 reference
stated in
PubMed
PubMed ID
19828734
retrieved
1 December 2016
title
The CORVET subunit Vps8 cooperates with the Rab5 homolog Vps21 to induce clustering of late endosomal compartments
(English)
1 reference
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PubMed
PubMed ID
19828734
retrieved
1 December 2016
main subject
cell biology
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CORVET complex membrane-binding subunit VPS8 YAL002W
1 reference
stated in
GOA release 2020-03-11
author
Janice Griffith
series ordinal
7
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Muriel Mari
series ordinal
4
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Fulvio Reggiori
series ordinal
8
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Christian Ungermann
series ordinal
9
object named as
Christian Ungermann
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author name string
Daniel F Markgraf
series ordinal
1
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Franziska Ahnert
series ordinal
2
0 references
Henning Arlt
series ordinal
3
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Karolina Peplowska
series ordinal
5
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Nadine Epp
series ordinal
6
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language of work or name
English
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publication date
December 2009
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published in
Molecular Biology of the Cell
1 reference
stated in
PubMed
PubMed ID
19828734
retrieved
1 December 2016
volume
20
0 references
issue
24
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page(s)
5276-89
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cites work
Membrane recruitment of the cargo-selective retromer subcomplex is catalysed by the small GTPase Rab7 and inhibited by the Rab-GAP TBC1D5
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Efficient termination of vacuolar Rab GTPase signaling requires coordinated action by a GAP and a protein kinase.
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Hrs and SNX3 functions in sorting and membrane invagination within multivesicular bodies
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Ypt1p is essential for retrograde Golgi-ER transport and for Golgi maintenance in S. cerevisiae.
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HOPS proofreads the trans-SNARE complex for yeast vacuole fusion
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The CORVET tethering complex interacts with the yeast Rab5 homolog Vps21 and is involved in endo-lysosomal biogenesis
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Dsl1p, Tip20p, and the novel Dsl3(Sec39) protein are required for the stability of the Q/t-SNARE complex at the endoplasmic reticulum in yeast
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Vps51p mediates the association of the GARP (Vps52/53/54) complex with the late Golgi t-SNARE Tlg1p
1 reference
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A novel phospholipid-binding protein from the yeast Saccharomyces cerevisiae with dual binding specificities for the transport GTPase Ypt7p and the Sec1-related Vps33p
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Retromer function in endosome-to-Golgi retrograde transport is regulated by the yeast Vps34 PtdIns 3-kinase
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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
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Pep3p/Pep5p complex: a putative docking factor at multiple steps of vesicular transport to the vacuole of Saccharomyces cerevisiae
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GRASP55, a second mammalian GRASP protein involved in the stacking of Golgi cisternae in a cell-free system.
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Vps9p is a guanine nucleotide exchange factor involved in vesicle-mediated vacuolar protein 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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Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae
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A novel RING finger protein, Vps8p, functionally interacts with the small GTPase, Vps21p, to facilitate soluble vacuolar protein localization
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A yeast protein related to a mammalian Ras-binding protein, Vps9p, is required for localization of vacuolar proteins
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A versatile toolbox for PCR-based tagging of yeast genes: new fluorescent proteins, more markers and promoter substitution cassettes
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Regulation of retromer recruitment to endosomes by sequential action of Rab5 and Rab7.
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Fab1p PtdIns(3)P 5-kinase function essential for protein sorting in the multivesicular body
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VPS27 controls vacuolar and endocytic traffic through a prevacuolar compartment in Saccharomyces cerevisiae
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Reconstitution of Rab- and SNARE-dependent membrane fusion by synthetic endosomes.
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1 reference
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1 reference
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reference URL
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29 September 2017
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1 reference
stated in
PubMed Central
reference URL
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1 reference
stated in
PubMed Central
reference URL
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29 September 2017
VPS21 controls entry of endocytosed and biosynthetic proteins into the yeast prevacuolar compartment.
1 reference
stated in
PubMed Central
reference URL
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1 reference
stated in
PubMed Central
reference URL
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29 September 2017
Genetic interaction with vps8-200 allows partial suppression of the vestigial vacuole phenotype caused by a pep5 mutation in Saccharomyces cerevisiae
1 reference
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PubMed Central
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PubMed Central
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29 September 2017
The Sec15 protein responds to the function of the GTP binding protein, Sec4, to control vesicular traffic in yeast
1 reference
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PubMed Central
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29 September 2017
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2 June 2018
Vps41 phosphorylation and the Rab Ypt7 control the targeting of the HOPS complex to endosome-vacuole fusion sites
1 reference
stated in
PubMed Central
reference URL
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2 June 2018
A cryosectioning procedure for the ultrastructural analysis and the immunogold labelling of yeast Saccharomyces cerevisiae
1 reference
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PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2793301
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2 June 2018
TRAPP stimulates guanine nucleotide exchange on Ypt1p
1 reference
stated in
PubMed Central
reference URL
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27 November 2018
New constructs and strategies for efficient PCR-based gene manipulations in yeast.
1 reference
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PubMed Central
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retrieved
27 November 2018
Mutations in the VPS45 gene, a SEC1 homologue, result in vacuolar protein sorting defects and accumulation of membrane vesicles
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2793301
retrieved
27 November 2018
A GTPase-activating protein controls Rab5 function in endocytic trafficking
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/19828734
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Identifiers
DOI
10.1091/MBC.E09-06-0521
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
1101519
OpenCitations bibliographic resource ID
1101519
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
1101519
PMCID
2793301
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
1101519
PubMed ID
19828734
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
1101519
ResearchGate publication ID
38011203
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