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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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scholarly article
1 reference
stated in
PubMed
PubMed ID
11994317
retrieved
1 December 2016
title
Sly1 protein bound to Golgi syntaxin Sed5p allows assembly and contributes to specificity of SNARE fusion complexes
(English)
1 reference
stated in
PubMed
PubMed ID
11994317
retrieved
1 December 2016
main subject
cell biology
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Sec17p YBL050W
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stated in
GOA release 2020-03-11
author name string
Renwang Peng
series ordinal
1
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Dieter Gallwitz
series ordinal
2
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language of work or name
English
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publication date
13 May 2002
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published in
Journal of Cell Biology
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stated in
PubMed
PubMed ID
11994317
retrieved
1 December 2016
volume
157
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page(s)
645-55
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issue
4
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cites work
Crystal structure of the endosomal SNARE complex reveals common structural principles of all SNAREs
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PubMed Central
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Vps45p stabilizes the syntaxin homologue Tlg2p and positively regulates SNARE complex formation
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Vam3p structure reveals conserved and divergent properties of syntaxins
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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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20 March 2017
Interactions within the yeast t-SNARE Sso1p that control SNARE complex assembly
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Topological restriction of SNARE-dependent membrane fusion
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Compartmental specificity of cellular membrane fusion encoded in SNARE proteins
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PubMed Central
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20 March 2017
A Ypt/Rab effector complex containing the Sec1 homolog Vps33p is required for homotypic vacuole fusion
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PubMed Central
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20 March 2017
Evidence for overlapping and distinct functions in protein transport of coat protein Sec24p family members
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PubMed Central
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20 March 2017
A conformational switch in syntaxin during exocytosis: role of munc18.
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20 March 2017
Sec1p binds to SNARE complexes and concentrates at sites of secretion
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PubMed Central
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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.
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20 March 2017
Conserved structural features of the synaptic fusion complex: SNARE proteins reclassified as Q- and R-SNAREs
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20 March 2017
Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 A resolution
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20 March 2017
Vesicular transport: how many Ypt/Rab-GTPases make a eukaryotic cell?
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20 March 2017
Ykt6p, a prenylated SNARE essential for endoplasmic reticulum-Golgi transport
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20 March 2017
Vam3p, a new member of syntaxin related protein, is required for vacuolar assembly in the yeast Saccharomyces cerevisiae
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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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t-SNARE activation through transient interaction with a rab-like guanosine triphosphatase
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20 March 2017
n-Sec1: a neural-specific syntaxin-binding protein
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PubMed Central
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20 March 2017
Identification and structure of four yeast genes (SLY) that are able to suppress the functional loss of YPT1, a member of the RAS superfamily
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20 March 2017
The yeast SLY gene products, suppressors of defects in the essential GTP-binding Ypt1 protein, may act in endoplasmic reticulum-to-Golgi transport
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20 March 2017
SED5 encodes a 39-kD integral membrane protein required for vesicular transport between the ER and the Golgi complex
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SNAP receptors implicated in vesicle targeting and fusion
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Selective interaction of complexin with the neuronal SNARE complex. Determination of the binding regions
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20 March 2017
Three-dimensional structure of the neuronal-Sec1-syntaxin 1a complex
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20 March 2017
Membrane fusion and exocytosis
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Synaptic assembly of the brain in the absence of neurotransmitter secretion
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7 April 2017
The diversity of Rab proteins in vesicle transport
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PubMed Central
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7 April 2017
Synaptic vesicle fusion complex contains unc-18 homologue bound to syntaxin
1 reference
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PubMed Central
reference URL
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7 April 2017
A rab protein is required for the assembly of SNARE complexes in the docking of transport vesicles
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PubMed Central
reference URL
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7 April 2017
Selective formation of Sed5p-containing SNARE complexes is mediated by combinatorial binding interactions.
1 reference
stated in
PubMed Central
reference URL
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Exocytosis requires asymmetry in the central layer of the SNARE complex
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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=2173853
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29 September 2017
Testing the 3Q:1R "rule": mutational analysis of the ionic "zero" layer in the yeast exocytic SNARE complex reveals no requirement for arginine
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PubMed Central
reference URL
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29 September 2017
Promiscuity in Rab-SNARE interactions
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=2173853
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29 September 2017
Specific interaction of the yeast cis-Golgi syntaxin Sed5p and the coat protein complex II component Sec24p of endoplasmic reticulum-derived transport 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=2173853
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29 September 2017
Bet1p activates the v-SNARE Bos1p
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=2173853
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29 September 2017
The molecular machinery for secretion is conserved from yeast to neurons
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=2173853
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29 September 2017
Secretion and cell-surface growth are blocked in a temperature-sensitive mutant of Saccharomyces cerevisiae
1 reference
stated in
PubMed Central
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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2173853
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29 September 2017
nSec1 binds a closed conformation of syntaxin1A.
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=2173853
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2 June 2018
SNARE interactions are not selective. Implications for membrane fusion specificity
1 reference
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PubMed Central
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2 June 2018
Homotypic vacuolar fusion mediated by t- and v-SNAREs.
1 reference
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PubMed Central
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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2173853
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2 June 2018
High-affinity binding of the yeast cis-Golgi t-SNARE, Sed5p, to wild-type and mutant Sly1p, a modulator of transport vesicle docking.
1 reference
stated in
Crossref
reference URL
https://api.crossref.org/works/10.1083%2FJCB.200202006
retrieved
21 January 2018
Distinct domains of syntaxin are required for synaptic vesicle fusion complex formation and dissociation.
1 reference
stated in
Crossref
reference URL
https://api.crossref.org/works/10.1083%2FJCB.200202006
retrieved
21 January 2018
The synaptic SNARE complex is a parallel four-stranded helical bundle
1 reference
stated in
Crossref
reference URL
https://api.crossref.org/works/10.1083%2FJCB.200202006
retrieved
21 January 2018
Rab GTPases, directors of vesicle docking.
1 reference
stated in
Crossref
reference URL
https://api.crossref.org/works/10.1083%2FJCB.200202006
retrieved
21 January 2018
The synaptobrevin-related domains of Bos1p and Sec22p bind to the syntaxin-like region of Sed5p
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/11994317
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Protein-protein interactions of the yeast Golgi t-SNARE Sed5 protein distinct from its neural plasma membrane cognate syntaxin 1
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/11994317
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Identifiers
DOI
10.1083/JCB.200202006
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
5002007
OpenCitations bibliographic resource ID
5002007
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
5002007
PMCID
2173853
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
5002007
PubMed ID
11994317
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
5002007
ResearchGate publication ID
11376846
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