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Functional specialization within a vesicle tethering complex: bypass of a subset of exocyst deletion mutants by Sec1p or Sec4p
scientific article
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scholarly article
1 reference
stated in
PubMed
PubMed ID
15583030
retrieved
1 December 2016
title
Functional specialization within a vesicle tethering complex: bypass of a subset of exocyst deletion mutants by Sec1p or Sec4p
(English)
1 reference
stated in
PubMed
PubMed ID
15583030
retrieved
1 December 2016
main subject
cell biology
0 references
GTP-Rho binding exocyst subunit EXO70 YJL085W
1 reference
stated in
GOA release 2020-03-11
GTP-Rho binding exocyst subunit SEC3 YER008C
1 reference
stated in
GOA release 2020-03-11
Exocyst subunit SEC5 YDR166C
1 reference
stated in
GOA release 2020-03-11
author
Susan Ferro-Novick
series ordinal
3
0 references
Johan-Owen De Craene
object named as
Johan-Owen De Craene
series ordinal
2
0 references
author name string
Andreas Wiederkehr
series ordinal
1
0 references
Peter Novick
series ordinal
4
0 references
language of work or name
English
0 references
publication date
6 December 2004
0 references
published in
Journal of Cell Biology
1 reference
stated in
PubMed
PubMed ID
15583030
retrieved
1 December 2016
volume
167
0 references
page(s)
875-87
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issue
5
0 references
cites work
Sec1p directly stimulates SNARE-mediated membrane fusion in vitro
1 reference
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PubMed Central
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Sec3p is needed for the spatial regulation of secretion and for the inheritance of the cortical endoplasmic reticulum
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20 March 2017
Vps51p links the VFT complex to the SNARE Tlg1p
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PubMed Central
reference URL
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Binding of Sly1 to Sed5 enhances formation of the yeast early Golgi SNARE complex
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Sly1 protein bound to Golgi syntaxin Sed5p allows assembly and contributes to specificity of SNARE fusion complexes
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Spatial regulation of the exocyst complex by Rho1 GTPase
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Ordering the final events in yeast exocytosis
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Class C Vps protein complex regulates vacuolar SNARE pairing and is required for vesicle docking/fusion
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A Ypt/Rab effector complex containing the Sec1 homolog Vps33p is required for homotypic vacuole fusion
1 reference
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PubMed Central
reference URL
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The Rho GTPase Rho3 has a direct role in exocytosis that is distinct from its role in actin polarity
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PubMed Central
reference URL
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Sec1p binds to SNARE complexes and concentrates at sites of secretion
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stated in
PubMed Central
reference URL
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20 March 2017
The exocyst is an effector for Sec4p, targeting secretory vesicles to sites of exocytosis
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PubMed Central
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Tropomyosin-containing actin cables direct the Myo2p-dependent polarized delivery of secretory vesicles in budding yeast
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Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae
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Sec3p is a spatial landmark for polarized secretion in budding yeast
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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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PubMed Central
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Analysis of a yeast SNARE complex reveals remarkable similarity to the neuronal SNARE complex and a novel function for the C terminus of the SNAP-25 homolog, Sec9.
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The Exocyst is a multiprotein complex required for exocytosis in Saccharomyces cerevisiae
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Sec6, Sec8, and Sec15 are components of a multisubunit complex which localizes to small bud tips in Saccharomyces cerevisiae
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SNAREpins: minimal machinery for membrane fusion
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PubMed Central
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20 March 2017
Vesicle tethering complexes in membrane traffic
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stated in
PubMed Central
reference URL
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20 March 2017
Sly1 binds to Golgi and ER syntaxins via a conserved N-terminal peptide motif
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PubMed Central
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Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae
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A ras-like protein is required for a post-Golgi event in yeast secretion
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SNARE Protein Structure and Function
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Vesicle trafficking: pleasure and pain from SM genes.
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Protein complexes in transport vesicle targeting
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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
reference URL
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retrieved
29 September 2017
The exocyst is a Ral effector complex
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/15583030
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Identifiers
DOI
10.1083/JCB.200408001
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
1774565
OpenCitations bibliographic resource ID
1774565
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
1774565
PMCID
2172455
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
1774565
PubMed ID
15583030
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
1774565
ResearchGate publication ID
8144954
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