Sec9 is a SNAP-25-like component of a yeast SNARE complex that may be the effector of Sec4 function in exocytosis.
about
Munc18-bound syntaxin readily forms SNARE complexes with synaptobrevin in native plasma membranesPhosphorylation of SNAP-23 by the novel kinase SNAK regulates t-SNARE complex assemblyInsulin-responsive tissues contain the core complex protein SNAP-25 (synaptosomal-associated protein 25) A and B isoforms in addition to syntaxin 4 and synaptobrevins 1 and 2Ascospore formation in the yeast Saccharomyces cerevisiae.The yeast par-1 homologs kin1 and kin2 show genetic and physical interactions with components of the exocytic machineryThe Exocyst is a multiprotein complex required for exocytosis in Saccharomyces cerevisiaeIn its active form, the GTP-binding protein rab8 interacts with a stress-activated protein kinaseTRAPP stably associates with the Golgi and is required for vesicle dockingGS32, a novel Golgi SNARE of 32 kDa, interacts preferentially with syntaxin 6The Rho GTPase Rho3 has a direct role in exocytosis that is distinct from its role in actin polarityConserved structural features of the synaptic fusion complex: SNARE proteins reclassified as Q- and R-SNAREsHigh-copy suppressor analysis reveals a physical interaction between Sec34p and Sec35p, a protein implicated in vesicle dockingrbSec1A and B colocalize with syntaxin 1 and SNAP-25 throughout the axon, but are not in a stable complex with syntaxinTwo new Ypt GTPases are required for exit from the yeast trans-Golgi compartmentERS-24, a mammalian v-SNARE implicated in vesicle traffic between the ER and the GolgiSEM1, a homologue of the split hand/split foot malformation candidate gene Dss1, regulates exocytosis and pseudohyphal differentiation in yeastThe Secret Life of Tethers: The Role of Tethering Factors in SNARE Complex RegulationThe Exocyst at a GlanceYeast VSM1 encodes a v-SNARE binding protein that may act as a negative regulator of constitutive exocytosis.A role for Tlg1p in the transport of proteins within the Golgi apparatus of Saccharomyces cerevisiaeThe critical role of Exo84p in the organization and polarized localization of the exocyst complex.Ordering the final events in yeast exocytosis.The GTPase Ypt7p of Saccharomyces cerevisiae is required on both partner vacuoles for the homotypic fusion step of vacuole inheritance.Regulation of SNARE complex assembly by an N-terminal domain of the t-SNARE Sso1p.Ric1p and the Ypt6p GTPase function in a common pathway required for localization of trans-Golgi network membrane proteinsThe polybasic juxtamembrane region of Sso1p is required for SNARE function in vivoSec1p directly stimulates SNARE-mediated membrane fusion in vitro.Sec3p is needed for the spatial regulation of secretion and for the inheritance of the cortical endoplasmic reticulum.The Exocyst Subunit Sec6 Interacts with Assembled Exocytic SNARE ComplexesMso1p: a yeast protein that functions in secretion and interacts physically and genetically with Sec1p.Involvement of long chain fatty acid elongation in the trafficking of secretory vesicles in yeastThe yeast lgl family member Sro7p is an effector of the secretory Rab GTPase Sec4p.Vam7p, a vacuolar SNAP-25 homolog, is required for SNARE complex integrity and vacuole docking and fusion.Prospore membrane formation defines a developmentally regulated branch of the secretory pathway in yeast.Btn2, a Hook1 ortholog and potential Batten disease-related protein, mediates late endosome-Golgi protein sorting in yeast.Molecular interactions position Mso1p, a novel PTB domain homologue, in the interface of the exocyst complex and the exocytic SNARE machinery in yeast.Docking of yeast vacuoles is catalyzed by the Ras-like GTPase Ypt7p after symmetric priming by Sec18p (NSF)The exocyst is an effector for Sec4p, targeting secretory vesicles to sites of exocytosis.A conserved domain is present in different families of vesicular fusion proteins: a new superfamilyMso1 is a novel component of the yeast exocytic SNARE complex.
P2860
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P2860
Sec9 is a SNAP-25-like component of a yeast SNARE complex that may be the effector of Sec4 function in exocytosis.
description
1994 nî lūn-bûn
@nan
1994 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1994 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
1994年の論文
@ja
1994年論文
@yue
1994年論文
@zh-hant
1994年論文
@zh-hk
1994年論文
@zh-mo
1994年論文
@zh-tw
1994年论文
@wuu
name
Sec9 is a SNAP-25-like compone ...... f Sec4 function in exocytosis.
@ast
Sec9 is a SNAP-25-like compone ...... f Sec4 function in exocytosis.
@en
Sec9 is a SNAP-25-like compone ...... f Sec4 function in exocytosis.
@nl
type
label
Sec9 is a SNAP-25-like compone ...... f Sec4 function in exocytosis.
@ast
Sec9 is a SNAP-25-like compone ...... f Sec4 function in exocytosis.
@en
Sec9 is a SNAP-25-like compone ...... f Sec4 function in exocytosis.
@nl
prefLabel
Sec9 is a SNAP-25-like compone ...... f Sec4 function in exocytosis.
@ast
Sec9 is a SNAP-25-like compone ...... f Sec4 function in exocytosis.
@en
Sec9 is a SNAP-25-like compone ...... f Sec4 function in exocytosis.
@nl
P2093
P3181
P1433
P1476
Sec9 is a SNAP-25-like compone ...... f Sec4 function in exocytosis.
@en
P2093
P304
P3181
P356
10.1016/0092-8674(94)90194-5
P407
P577
1994-10-21T00:00:00Z