COPII subunit interactions in the assembly of the vesicle coat. - Wikidata - awgldk - TriplyDB

COPII subunit interactions in the assembly of the vesicle coat.

COPII subunit interactions in the assembly of the vesicle coat.

http://www.wikidata.org/entity/Q27931462

about

Hypothetical protein KIAA0079 is a mammalian homologue of yeast Sec24p p125 is a novel mammalian Sec23p-interacting protein with structural similarity to phospholipid-modifying proteins Mammalian homologues of yeast sec31p. An ubiquitously expressed form is localized to endoplasmic reticulum (ER) exit sites and is essential for ER-Golgi transport Sec16B is involved in the endoplasmic reticulum export of the peroxisomal membrane biogenesis factor peroxin 16 (Pex16) in mammalian cells Assembly, organization, and function of the COPII coat Insights into COPII coat nucleation from the structure of Sec23.Sar1 complexed with the active fragment of Sec31 Sec16 defines endoplasmic reticulum exit sites and is required for secretory cargo export in mammalian cells Two mammalian Sec16 homologues have nonredundant functions in endoplasmic reticulum (ER) export and transitional ER organization Vesicle-mediated ER export of proteins and lipids Molecular mechanisms of Sar/Arf GTPases in vesicular trafficking in yeast and plants Structure of the Sec23/24-Sar1 pre-budding complex of the COPII vesicle coat Structure of the Sec13–Sec16 edge element, a template for assembly of the COPII vesicle coat The Structure of Sec12 Implicates Potassium Ion Coordination in Sar1 Activation Sec16 influences transitional ER sites by regulating rather than organizing COPII.Smy2p participates in COPII vesicle formation through the interaction with Sec23p/Sec24p subcomplex.The alpha- and beta'-COP WD40 domains mediate cargo-selective interactions with distinct di-lysine motifs.Sec16p potentiates the action of COPII proteins to bud transport vesicles Insights into structural and regulatory roles of Sec16 in COPII vesicle formation at ER exit sites.Sfb2p, a yeast protein related to Sec24p, can function as a constituent of COPII coats required for vesicle budding from the endoplasmic reticulum.Aut7p, a soluble autophagic factor, participates in multiple membrane trafficking processes.Sec24p and Iss1p function interchangeably in transport vesicle formation from the endoplasmic reticulum in Saccharomyces cerevisiae.Shr3p mediates specific COPII coatomer-cargo interactions required for the packaging of amino acid permeases into ER-derived transport vesicles Nucleus-vacuole junctions in Saccharomyces cerevisiae are formed through the direct interaction of Vac8p with Nvj1p.Sec12 binds to Sec16 at transitional ER sites A membrane protein enriched in endoplasmic reticulum exit sites interacts with COPII Identification of the putative mammalian orthologue of Sec31P, a component of the COPII coat.Structure of the Sec23p/24p and Sec13p/31p complexes of COPII Vesicular calcium regulates coat retention, fusogenicity, and size of pre-Golgi intermediates.Genetic analysis of yeast Sec24p mutants suggests cargo binding is not co-operative during ER export.Regulation of coat assembly--sorting things out at the ER.p125A exists as part of the mammalian Sec13/Sec31 COPII subcomplex to facilitate ER-Golgi transport.Functional morphology of the secretory pathway organelles in yeast.Apoptosis-linked gene-2 (ALG-2)/Sec31 interactions regulate endoplasmic reticulum (ER)-to-Golgi transport: a potential effector pathway for luminal calcium The use of yeast two-hybrid screens in studies of protein:protein interactions involved in trafficking.Characterization of human Sec16B: indications of specialized, non-redundant functions Structure of the Sec13/31 COPII coat cage.CK2 phosphorylates Sec31 and regulates ER-To-Golgi trafficking Mammalian Sec16/p250 plays a role in membrane traffic from the endoplasmic reticulum.Structural disorder provides increased adaptability for vesicle trafficking pathways.Sec24p and Sec16p cooperate to regulate the GTP cycle of the COPII coat.

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P2860

COPII subunit interactions in the assembly of the vesicle coat.

http://www.wikidata.org/entity/Q27931462

description

1997 nî lūn-bûn

@nan

1997 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

@hyw

1997 թվականի հոտեմբերին հրատարակված գիտական հոդված

@hy

1997年の論文

@ja

1997年論文

@yue

1997年論文

@zh-hant

1997年論文

@zh-hk

1997年論文

@zh-mo

1997年論文

@zh-tw

1997年论文

@wuu

name

COPII subunit interactions in the assembly of the vesicle coat.

@ast

COPII subunit interactions in the assembly of the vesicle coat.

@en

COPII subunit interactions in the assembly of the vesicle coat.

@nl

type

label

COPII subunit interactions in the assembly of the vesicle coat.

@ast

COPII subunit interactions in the assembly of the vesicle coat.

@en

COPII subunit interactions in the assembly of the vesicle coat.

@nl

prefLabel

COPII subunit interactions in the assembly of the vesicle coat.

@ast

COPII subunit interactions in the assembly of the vesicle coat.

@en

COPII subunit interactions in the assembly of the vesicle coat.

@nl

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JBC.272.41.25413

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Journal of Biological Chemistry

P1476

COPII subunit interactions in the assembly of the vesicle coat.

@en

P2093

C A Kaiser

http://www.w3.org/2001/XMLSchema#string

D A Shaywitz

http://www.w3.org/2001/XMLSchema#string

P J Espenshade

http://www.w3.org/2001/XMLSchema#string

R E Gimeno

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P2860

Molecular characterization of a novel human gene, SEC13R, related to the yeast secretory pathway gene SEC13, and mapping to a conserved linkage group on human chromosome 3p24-p25 and mouse chromosome 6

Cloning and functional characterization of mammalian homologues of the COPII component Sec23

Cdi1, a human G1 and S phase protein phosphatase that associates with Cdk2

Human SEC13Rp functions in yeast and is located on transport vesicles budding from the endoplasmic reticulum

Mammalian Ras interacts directly with the serine/threonine kinase Raf

A novel genetic system to detect protein-protein interactions

COPII: a membrane coat formed by Sec proteins that drive vesicle budding from the endoplasmic reticulum.

Yeast SEC16 gene encodes a multidomain vesicle coat protein that interacts with Sec23p

Cytosolic Sec13p complex is required for vesicle formation from the endoplasmic reticulum in vitro.

SED4 encodes a yeast endoplasmic reticulum protein that binds Sec16p and participates in vesicle formation.

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25413-6

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10.1074/JBC.272.41.25413

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41

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272

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1997-10-10T00:00:00Z

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13901673

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