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Yeast homotypic vacuole fusion requires the Ccz1-Mon1 complex during the tethering/docking stage
scientific article
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instance of
scholarly article
1 reference
stated in
PubMed
PubMed ID
14662743
retrieved
1 December 2016
title
Yeast homotypic vacuole fusion requires the Ccz1-Mon1 complex during the tethering/docking stage
(English)
1 reference
stated in
PubMed
PubMed ID
14662743
retrieved
1 December 2016
main subject
cell biology
0 references
Ccz1p YBR131W
1 reference
stated in
GOA release 2020-03-11
Mon1p YGL124C
1 reference
stated in
GOA release 2020-03-11
vacuole
1 reference
based on heuristic
inferred from title
author
Daniel J. Klionsky
series ordinal
5
object named as
Daniel J Klionsky
0 references
author name string
Chao-Wen Wang
series ordinal
1
0 references
Per E Stromhaug
series ordinal
2
0 references
Emily J Kauffman
series ordinal
3
0 references
Lois S Weisman
series ordinal
4
0 references
language of work or name
English
0 references
publication date
8 December 2003
0 references
published in
Journal of Cell Biology
1 reference
stated in
PubMed
PubMed ID
14662743
retrieved
1 December 2016
volume
163
0 references
issue
5
0 references
page(s)
973-85
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cites work
Vam10p defines a Sec18p-independent step of priming that allows yeast vacuole tethering
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=1705953
retrieved
20 March 2017
Vps51 is part of the yeast Vps fifty-three tethering complex essential for retrograde traffic from the early endosome and Cvt vesicle completion
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=1705953
retrieved
20 March 2017
The Ccz1-Mon1 protein complex is required for the late step of multiple vacuole delivery pathways
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=1705953
retrieved
20 March 2017
Vacuole fusion at a ring of vertex docking sites leaves membrane fragments within the organelle
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=1705953
retrieved
20 March 2017
The Ccz1 protein interacts with Ypt7 GTPase during fusion of multiple transport intermediates with the vacuole in S. cerevisiae.
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=1705953
retrieved
20 March 2017
Fusion of docked membranes requires the armadillo repeat protein Vac8p
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=1705953
retrieved
20 March 2017
Apg2 is a novel protein required for the cytoplasm to vacuole targeting, autophagy, and pexophagy pathways
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=1705953
retrieved
20 March 2017
Cvt9/Gsa9 functions in sequestering selective cytosolic cargo destined for the vacuole
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=1705953
retrieved
20 March 2017
The novel protein Ccz1p required for vacuolar assembly in Saccharomyces cerevisiae functions in the same transport pathway as Ypt7p
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=1705953
retrieved
20 March 2017
New component of the vacuolar class C-Vps complex couples nucleotide exchange on the Ypt7 GTPase to SNARE-dependent docking and fusion
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=1705953
retrieved
20 March 2017
Class C Vps protein complex regulates vacuolar SNARE pairing and is required for vesicle docking/fusion
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=1705953
retrieved
20 March 2017
Compartmental specificity of cellular membrane fusion encoded in SNARE proteins
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=1705953
retrieved
20 March 2017
Three v-SNAREs and two t-SNAREs, present in a pentameric cis-SNARE complex on isolated vacuoles, are essential for homotypic fusion.
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=1705953
retrieved
20 March 2017
Vam7p, a vacuolar SNAP-25 homolog, is required for SNARE complex integrity and vacuole docking and fusion
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=1705953
retrieved
20 March 2017
A vacuolar v-t-SNARE complex, the predominant form in vivo and on isolated vacuoles, is disassembled and activated for docking and fusion
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=1705953
retrieved
20 March 2017
Protein sorting in Saccharomyces cerevisiae: isolation of mutants defective in the delivery and processing of multiple vacuolar hydrolases
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=1705953
retrieved
20 March 2017
Genomic libraries and a host strain designed for highly efficient two-hybrid selection in yeast
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=1705953
retrieved
20 March 2017
Sec18p (NSF)-driven release of Sec17p (alpha-SNAP) can precede docking and fusion of yeast vacuoles
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=1705953
retrieved
20 March 2017
A cycle of Vam7p release from and PtdIns 3-P-dependent rebinding to the yeast vacuole is required for homotypic vacuole fusion
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=1705953
retrieved
29 September 2017
Yeast vacuoles and membrane fusion pathways
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=1705953
retrieved
29 September 2017
Convergence of multiple autophagy and cytoplasm to vacuole targeting components to a perivacuolar membrane compartment prior to de novo vesicle formation
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=1705953
retrieved
29 September 2017
Yeast homotypic vacuole fusion: a window on organelle trafficking mechanisms
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=1705953
retrieved
29 September 2017
A Structural Change Occurs upon Binding of Syntaxin to SNAP-25
1 reference
stated in
Crossref
reference URL
https://api.crossref.org/works/10.1083%2FJCB.200308071
retrieved
21 January 2018
Identifiers
DOI
10.1083/JCB.200308071
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
431916
OpenCitations bibliographic resource ID
431916
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
431916
PMCID
1705953
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
431916
PubMed ID
14662743
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
431916
ResearchGate publication ID
8969870
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