A rat brain Sec1 homologue related to Rop and UNC18 interacts with syntaxin
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VAMP-7 mediates vesicular transport from endosomes to lysosomesThree novel proteins of the syntaxin/SNAP-25 familyYkt6p, a prenylated SNARE essential for endoplasmic reticulum-Golgi transportMutations in VPS33B, encoding a regulator of SNARE-dependent membrane fusion, cause arthrogryposis-renal dysfunction-cholestasis (ARC) syndromeDirect interaction between the COG complex and the SM protein, Sly1, is required for Golgi SNARE pairingThe Exocyst is a multiprotein complex required for exocytosis in Saccharomyces cerevisiaerbSec1A and B colocalize with syntaxin 1 and SNAP-25 throughout the axon, but are not in a stable complex with syntaxinMunc18-1 binds directly to the neuronal SNARE complexDistinct initial SNARE configurations underlying the diversity of exocytosisDynamic conformational changes in munc18 prevent syntaxin bindingStructural basis for the Golgi membrane recruitment of Sly1p by Sed5p.Yeast VSM1 encodes a v-SNARE binding protein that may act as a negative regulator of constitutive exocytosis.Regulation of SNARE complex assembly by an N-terminal domain of the t-SNARE Sso1p.Genetic interactions between a pep7 mutation and the PEP12 and VPS45 genes: evidence for a novel SNARE component in transport between the Saccharomyces cerevisiae Golgi complex and endosome.A multispecificity syntaxin homologue, Vam3p, essential for autophagic and biosynthetic protein transport to the vacuole.A novel RING finger protein complex essential for a late step in protein transport to the yeast vacuoleStructure-based functional analysis reveals a role for the SM protein Sly1p in retrograde transport to the endoplasmic reticulum.Biochemical requirements for the targeting and fusion of ER-derived transport vesicles with purified yeast Golgi membranes.Sec1p binds to SNARE complexes and concentrates at sites of secretionAut7p, a soluble autophagic factor, participates in multiple membrane trafficking processes.Three-dimensional structure of the neuronal-Sec1-syntaxin 1a complexDistinct Rab binding specificity of Rim1, Rim2, rabphilin, and Noc2. Identification of a critical determinant of Rab3A/Rab27A recognition by Rim2Slp4-a/granuphilin-a inhibits dense-core vesicle exocytosis through interaction with the GDP-bound form of Rab27A in PC12 cellsRegulation of Munc-18/syntaxin 1A interaction by cyclin-dependent kinase 5 in nerve endingsA role of amphiphysin in synaptic vesicle endocytosis suggested by its binding to dynamin in nerve terminalsPhosphorylation of Munc-18/n-Sec1/rbSec1 by protein kinase C: its implication in regulating the interaction of Munc-18/n-Sec1/rbSec1 with syntaxinMammalian homologues of Caenorhabditis elegans unc-13 gene define novel family of C2-domain proteinsRegulation of exocytosis by cyclin-dependent kinase 5 via phosphorylation of Munc18Direct interaction of the rat unc-13 homologue Munc13-1 with the N terminus of syntaxinMunc18c depletion selectively impairs the sustained phase of insulin releaseIdentification of a mammalian Golgi Sec1p-like protein, mVps45AQP2 exocytosis in the renal collecting duct -- involvement of SNARE isoforms and the regulatory role of Munc18bMammalian Sly1 regulates syntaxin 5 function in endoplasmic reticulum to Golgi transportMunc18b is an essential gene in mice whose expression is limiting for secretion by airway epithelial and mast cellsVesicle fusion probability is determined by the specific interactions of munc18The V0 sector of the V-ATPase, synaptobrevin, and synaptophysin are associated on synaptic vesicles in a Triton X-100-resistant, freeze-thawing sensitive, complexAdipocytes from Munc18c-null mice show increased sensitivity to insulin-stimulated GLUT4 externalizationA novel isoform of syntaxin-binding protein homologous to yeast Sec1 expressed ubiquitously in mammalian cellsA Novel Ubiquitous Form of Munc-18 Interacts with Multiple Syntaxins.Munc-18-1 inhibits phospholipase D activity by direct interaction in an epidermal growth factor-reversible manner.
P2860
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P2860
A rat brain Sec1 homologue related to Rop and UNC18 interacts with syntaxin
description
1994 nî lūn-bûn
@nan
1994 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
1994 թվականի մարտին հրատարակված գիտական հոդված
@hy
1994年の論文
@ja
1994年学术文章
@wuu
1994年学术文章
@zh-cn
1994年学术文章
@zh-hans
1994年学术文章
@zh-my
1994年学术文章
@zh-sg
1994年學術文章
@yue
name
A rat brain Sec1 homologue related to Rop and UNC18 interacts with syntaxin
@ast
A rat brain Sec1 homologue related to Rop and UNC18 interacts with syntaxin
@en
type
label
A rat brain Sec1 homologue related to Rop and UNC18 interacts with syntaxin
@ast
A rat brain Sec1 homologue related to Rop and UNC18 interacts with syntaxin
@en
prefLabel
A rat brain Sec1 homologue related to Rop and UNC18 interacts with syntaxin
@ast
A rat brain Sec1 homologue related to Rop and UNC18 interacts with syntaxin
@en
P2093
P2860
P356
P1476
A rat brain Sec1 homologue related to Rop and UNC18 interacts with syntaxin
@en
P2093
P2860
P304
P356
10.1073/PNAS.91.6.2003
P407
P577
1994-03-01T00:00:00Z