Protein interactions regulating vesicle transport between the endoplasmic reticulum and Golgi apparatus in mammalian cells
about
Three novel proteins of the syntaxin/SNAP-25 familySyntaxin 18, a SNAP receptor that functions in the endoplasmic reticulum, intermediate compartment, and cis-Golgi vesicle traffickingSyntaxin 17 is abundant in steroidogenic cells and implicated in smooth endoplasmic reticulum membrane dynamicsAssociation of a novel PDZ domain-containing peripheral Golgi protein with the Q-SNARE (Q-soluble N-ethylmaleimide-sensitive fusion protein (NSF) attachment protein receptor) protein syntaxin 6Participation of the syntaxin 5/Ykt6/GS28/GS15 SNARE complex in transport from the early/recycling endosome to the trans-Golgi networkSyntaxin 16 and syntaxin 5 are required for efficient retrograde transport of several exogenous and endogenous cargo proteinsVesicle-associated membrane protein 7 is expressed in intestinal ERA novel synaptobrevin/VAMP homologous protein (VAMP5) is increased during in vitro myogenesis and present in the plasma membraneAutophagic substrate clearance requires activity of the syntaxin-5 SNARE complexDistinct SNARE complexes mediating membrane fusion in Golgi transport based on combinatorial specificity.CASP, the alternatively spliced product of the gene encoding the CCAAT-displacement protein transcription factor, is a Golgi membrane protein related to giantinB cells promote insulin resistance through modulation of T cells and production of pathogenic IgG antibodiesrsly1 binding to syntaxin 5 is required for endoplasmic reticulum-to-Golgi transport but does not promote SNARE motif accessibilityGS32, a novel Golgi SNARE of 32 kDa, interacts preferentially with syntaxin 6Vesicle-associated membrane protein 4 is implicated in trans-Golgi network vesicle traffickingSequential tethering of Golgins and catalysis of SNAREpin assembly by the vesicle-tethering protein p115The mammalian protein (rbet1) homologous to yeast Bet1p is primarily associated with the pre-Golgi intermediate compartment and is involved in vesicular transport from the endoplasmic reticulum to the Golgi apparatusTargeting of Arf-1 to the early Golgi by membrin, an ER-Golgi SNARELocalization, dynamics, and protein interactions reveal distinct roles for ER and Golgi SNAREsSyntaxin 13 mediates cycling of plasma membrane proteins via tubulovesicular recycling endosomesA novel snare N-terminal domain revealed by the crystal structure of Sec22bCrystal structure of SEDL and its implications for a genetic disease spondyloepiphyseal dysplasia tardaCoupled ER to Golgi transport reconstituted with purified cytosolic proteinsA role for Tlg1p in the transport of proteins within the Golgi apparatus of Saccharomyces cerevisiaeCharacterization of a novel yeast SNARE protein implicated in Golgi retrograde trafficAsymmetric requirements for a Rab GTPase and SNARE proteins in fusion of COPII vesicles with acceptor membranesVam7p, a vacuolar SNAP-25 homolog, is required for SNARE complex integrity and vacuole docking and fusion.Two syntaxin homologues in the TGN/endosomal system of yeastSyntaxin 13 is a developmentally regulated SNARE involved in neurite outgrowth and endosomal traffickingSubunit structure of a mammalian ER/Golgi SNARE complexThe p115-interactive proteins GM130 and giantin participate in endoplasmic reticulum-Golgi trafficYkt6 forms a SNARE complex with syntaxin 5, GS28, and Bet1 and participates in a late stage in endoplasmic reticulum-Golgi transportLegionella pneumophila regulates the small GTPase Rab1 activity by reversible phosphorylcholinationAn isoform of the Golgi t-SNARE, syntaxin 5, with an endoplasmic reticulum retrieval signalThe SNARE motif contributes to rbet1 intracellular targeting and dynamics independently of SNARE interactionsSyntaxin 6 functions in trans-Golgi network vesicle traffickingGS15, a 15-kilodalton Golgi soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) homologous to rbet1Mammalian ykt6 is a neuronal SNARE targeted to a specialized compartment by its profilin-like amino terminal domainR-SNARE ykt6 resides in membrane-associated protease-resistant protein particles and modulates cell cycle progression when over-expressedMapping of R-SNARE function at distinct intracellular GLUT4 trafficking steps in adipocytes
P2860
0ce86586f9768468cfa03d8ba017004b3763f4854ad8df320fdfefdf1015de6bef93c1f659ef2871628e03f557f52b95a269d3631fa9ba21183d7ed462e96cdb1a84870d79b0a2c8c844768f59a363a97588052a25972ab1af7ac274b1bbdec3702f4bb97eadf672ad700fefb1ab4a3dbef569245d3d8640950f58ef4fe79ee45903cd7b27bedb7d3ddb0f5f9ee64e6bdb674ffda4ec072882a4bd1f0504b760c07897020ffd39e760951b86699435a98737a533cd54ea4f04a684c051ce664bcb8bd1fab12fcc7b
P248
Q22008531-52ED9393-D05F-4CB4-8EA9-536D80504D6EQ22254009-16585B53-EAFD-4A6A-BBAC-F79AE240747CQ22254741-02F4FB88-049F-48A3-80A2-0F43CE8E19A2Q24291274-3B473B1E-75B4-4701-B9BE-0D04025645C6Q24297647-001DCADF-E4C7-47A0-B453-B9F15F78F89AQ24301008-EA16B9A8-3EDB-4AC8-8643-5B000C62A17DQ24305479-37B6956C-0307-49DB-BDC7-1C419247E5DBQ24310308-200E707D-48EB-497E-B7C0-41171BB12BEDQ24337387-B9572614-592A-4B32-8487-542410C9E37EQ24534126-24F5C0E3-E3C4-46E4-B5A4-D1598E784A30Q24537148-C917686F-A9C2-48E7-BFE0-7F9CD4EACF07Q24598772-76C465A4-BE90-4E99-86AE-E2866567FEBDQ24619563-EDB507F1-6F47-4A91-8222-D2E5C8F66885Q24644645-836CD657-6D5A-4F45-BC59-C3331CC22D12Q24649038-6FD9092F-5C48-4401-8BE0-696F6F7A2E93Q24673491-63CD26F2-316E-4F69-B3BC-5FA39412A676Q24677983-D3188D93-C124-4F8B-8700-9D984CF220CAQ24678419-AC52E4B6-9B5F-4335-81E5-C4653E1C4908Q24682651-B59EB0F3-5763-444F-8779-68EF76DC3AC1Q24682732-DE135DEB-90DA-45F9-8D00-6C4A07DC0972Q27631238-5A6EB9C0-95C3-4E80-AB27-B838269A482CQ27639734-9C131728-825C-473A-9E83-5FA36AD8A6C5Q27929807-50AAE08F-1EC1-4680-A71C-7C3BB3D33852Q27930001-DC6B3867-9B1B-4259-9E97-B6C88E5925F5Q27930083-49283523-8063-42F7-B8BC-572D09506BFFQ27932451-78838F39-398A-42A5-956A-48FC9DFB76A1Q27933694-F40C2220-754F-425C-A9F2-D86DCE2CD110Q27937369-18332773-9CDC-4A5F-B983-2A4F00493B8EQ28140261-61F02D85-91CB-4D98-9D4B-D2B5CC74CD0EQ28141448-09FDA2A1-E6EE-4952-8F7A-92768AC436CEQ28141461-E2F6E4CA-0D7D-4C49-A402-90D82B9DA8ADQ28185724-F2FBAB7D-B3AA-4F4F-8FEB-3B35052B5873Q28485632-FAD51FF4-8E97-4241-9BCB-82C370264DA2Q28570066-182A1C3E-A2AE-46DD-94F9-59226E986FADQ28571014-DB515E46-8F20-4195-A91A-BA4BE3350FBEQ28572919-052F66C2-DDFA-4F9E-A5F2-5E9EEBA196A9Q28579141-1B9774D7-014D-45C1-A160-215B552E6BC5Q28579640-CCB5053D-23F6-4A40-8A3C-112CC6B91AE4Q28580997-B43C68C8-1E13-4CED-8893-33642440AA26Q28591768-42C10E93-0783-49A0-8876-D67D4C85E242
P2860
Protein interactions regulating vesicle transport between the endoplasmic reticulum and Golgi apparatus in mammalian cells
description
1997 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
1997 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 1997
@ast
im April 1997 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 1997/04/04)
@sk
vědecký článek publikovaný v roce 1997
@cs
wetenschappelijk artikel (gepubliceerd op 1997/04/04)
@nl
наукова стаття, опублікована у квітні 1997
@uk
مقالة علمية (نشرت في 4-4-1997)
@ar
name
Protein interactions regulatin ...... i apparatus in mammalian cells
@ast
Protein interactions regulatin ...... i apparatus in mammalian cells
@en
Protein interactions regulatin ...... i apparatus in mammalian cells
@nl
type
label
Protein interactions regulatin ...... i apparatus in mammalian cells
@ast
Protein interactions regulatin ...... i apparatus in mammalian cells
@en
Protein interactions regulatin ...... i apparatus in mammalian cells
@nl
prefLabel
Protein interactions regulatin ...... i apparatus in mammalian cells
@ast
Protein interactions regulatin ...... i apparatus in mammalian cells
@en
Protein interactions regulatin ...... i apparatus in mammalian cells
@nl
P2093
P921
P3181
P1433
P1476
Protein interactions regulatin ...... i apparatus in mammalian cells
@en
P2093
D. S. Chao
R. H. Scheller
P304
P3181
P356
10.1016/S0092-8674(00)80191-9
P407
P577
1997-04-04T00:00:00Z