Coatomer interaction with di-lysine endoplasmic reticulum retention motifs
about
Retention of subunits of the oligosaccharyltransferase complex in the endoplasmic reticulumSyntaxin 18, a SNAP receptor that functions in the endoplasmic reticulum, intermediate compartment, and cis-Golgi vesicle traffickingEndoplasmic reticulum localization of Gaa1 and PIG-T, subunits of the glycosylphosphatidylinositol transamidase complexThe human phosphatidylinositol phosphatase SAC1 interacts with the coatomer I complexNovel isotypic gamma/zeta subunits reveal three coatomer complexes in mammalsThe cargo receptors Surf4, endoplasmic reticulum-Golgi intermediate compartment (ERGIC)-53, and p25 are required to maintain the architecture of ERGIC and Golgi.COOH-terminal sequence motifs target the T cell protein tyrosine phosphatase to the ER and nucleusScyl1, mutated in a recessive form of spinocerebellar neurodegeneration, regulates COPI-mediated retrograde trafficRGS4 and RGS2 bind coatomer and inhibit COPI association with Golgi membranes and intracellular transportHigh-content screening microscopy identifies novel proteins with a putative role in secretory membrane trafficIncomplete endoplasmic reticulum (ER) retention in immature thymocytes as revealed by surface expression of "ER-resident" molecular chaperonesNon-clathrin-coat protein alpha is a conserved subunit of coatomer and in Saccharomyces cerevisiae is essential for growthCOP I domains required for coatomer integrity, and novel interactions with ARF and ARF-GAPMaintenance of Golgi structure and function depends on the integrity of ER exportEvidence that the entire Golgi apparatus cycles in interphase HeLa cells: sensitivity of Golgi matrix proteins to an ER exit blockERGIC-53 is a functional mannose-selective and calcium-dependent human homologue of leguminous lectinsA major transmembrane protein of Golgi-derived COPI-coated vesicles involved in coatomer bindingArchitecture of coatomer: molecular characterization of delta-COP and protein interactions within the complexSorting by COP I-coated vesicles under interphase and mitotic conditionsARFGAP1 promotes the formation of COPI vesicles, suggesting function as a component of the coatMannose 6-phosphate receptors regulate the formation of clathrin-coated vesicles in the TGNFunctional reconstitution of COPI coat assembly and disassembly using chemically defined componentsA single binding site for dilysine retrieval motifs and p23 within the gamma subunit of coatomerA role for giantin in docking COPI vesicles to Golgi membranesReversible dissociation of coatomer: functional characterization of a beta/delta-coat protein subcomplexEndoplasmic reticulum chaperones and oxidoreductases: critical regulators of tumor cell survival and immunorecognitionCOPI budding within the Golgi stackMalectin: A Novel Carbohydrate-binding Protein of the Endoplasmic Reticulum and a Candidate Player in the Early Steps of Protein N-GlycosylationMolecular Basis for Recognition of Dilysine Trafficking Motifs by COPIRules for the recognition of dilysine retrieval motifs by coatomerReceptor-induced polymerization of coatomerYeast functional analysis: identification of two essential genes involved in ER to Golgi trafficking.Novel Golgi to vacuole delivery pathway in yeast: identification of a sorting determinant and required transport component.Endoplasmic reticulum localization of Sec12p is achieved by two mechanisms: Rer1p-dependent retrieval that requires the transmembrane domain and Rer1p-independent retention that involves the cytoplasmic domain.Rer1p, a retrieval receptor for endoplasmic reticulum membrane proteins, is dynamically localized to the Golgi apparatus by coatomerDeubiquitination, a new player in Golgi to endoplasmic reticulum retrograde transport.The alpha- and beta'-COP WD40 domains mediate cargo-selective interactions with distinct di-lysine motifs.Rer1p as common machinery for the endoplasmic reticulum localization of membrane proteins.Reconstitution of coat protein complex II (COPII) vesicle formation from cargo-reconstituted proteoliposomes reveals the potential role of GTP hydrolysis by Sar1p in protein sorting.Reconstitution of retrograde transport from the Golgi to the ER in vitro.
P2860
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P2860
Coatomer interaction with di-lysine endoplasmic reticulum retention motifs
description
1994 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
1994 թվականի մարտին հրատարակված գիտական հոդված
@hy
article publié dans la revue scientifique Science
@fr
artículu científicu espublizáu en 1994
@ast
im März 1994 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 1994/03/18)
@sk
vědecký článek publikovaný v roce 1994
@cs
wetenschappelijk artikel (gepubliceerd op 1994/03/18)
@nl
наукова стаття, опублікована в березні 1994
@uk
name
Coatomer interaction with di-lysine endoplasmic reticulum retention motifs
@ast
Coatomer interaction with di-lysine endoplasmic reticulum retention motifs
@en
Coatomer interaction with di-lysine endoplasmic reticulum retention motifs
@nl
type
label
Coatomer interaction with di-lysine endoplasmic reticulum retention motifs
@ast
Coatomer interaction with di-lysine endoplasmic reticulum retention motifs
@en
Coatomer interaction with di-lysine endoplasmic reticulum retention motifs
@nl
prefLabel
Coatomer interaction with di-lysine endoplasmic reticulum retention motifs
@ast
Coatomer interaction with di-lysine endoplasmic reticulum retention motifs
@en
Coatomer interaction with di-lysine endoplasmic reticulum retention motifs
@nl
P3181
P356
P1433
P1476
Coatomer interaction with di-lysine endoplasmic reticulum retention motifs
@en
P2093
F. Letourneur
P304
P3181
P356
10.1126/SCIENCE.8128252
P407
P577
1994-03-18T00:00:00Z