ARF-GAP-mediated interaction between the ER-Golgi v-SNAREs and the COPI coat. - Wikidata - awgldk - TriplyDB

ARF-GAP-mediated interaction between the ER-Golgi v-SNAREs and the COPI coat.

ARF-GAP-mediated interaction between the ER-Golgi v-SNAREs and the COPI coat.

http://www.wikidata.org/entity/Q42917503

about

Dynamics of GBF1, a Brefeldin A-sensitive Arf1 exchange factor at the Golgi Targeting of Arf-1 to the early Golgi by membrin, an ER-Golgi SNARE Functional reconstitution of COPI coat assembly and disassembly using chemically defined components Coat/Tether Interactions-Exception or Rule?The cytoskeletal arrangements necessary to neurogenesis The non-catalytic carboxyl-terminal domain of ARFGAP1 regulates actin cytoskeleton reorganization by antagonizing the activation of Rac1 Suppression of coatomer mutants by a new protein family with COPI and COPII binding motifs in Saccharomyces cerevisiae.The Gcs1 Arf-GAP mediates Snc1,2 v-SNARE retrieval to the Golgi in yeast.The ArfGAP Glo3 is required for the generation of COPI vesicles.The SNARE motif contributes to rbet1 intracellular targeting and dynamics independently of SNARE interactions Sorting in early endosomes reveals connections to docking- and fusion-associated factors Arf GAPs: gatekeepers of vesicle generation.Organization of SNAREs within the Golgi stack A complete set of SNAREs in yeast.Models for the functions of Arf GAPs.α-Synuclein and ALPS motifs are membrane curvature sensors whose contrasting chemistry mediates selective vesicle binding.ER-to-Golgi transport: COP I and COP II function (Review).Biological functions of phosphatidylinositol transfer proteins.Sec24- and ARFGAP1-dependent trafficking of GABA transporter-1 is a prerequisite for correct axonal targeting.The Sec14-superfamily and the regulatory interface between phospholipid metabolism and membrane trafficking The ArfGAP2/3 Glo3 and ergosterol collaborate in transport of a subset of cargoes.ARFGAP1 plays a central role in coupling COPI cargo sorting with vesicle formation.ArfGAP1 dynamics and its role in COPI coat assembly on Golgi membranes of living cells.The yeast p24 complex is required for the formation of COPI retrograde transport vesicles from the Golgi apparatus.Characterization of class I and II ADP-ribosylation factors (Arfs) in live cells: GDP-bound class II Arfs associate with the ER-Golgi intermediate compartment independently of GBF1.Retrograde traffic from the Golgi to the endoplasmic reticulum.The cystic fibrosis transmembrane conductance regulator's expanding SNARE interactome.Entry and exit mechanisms at the cis-face of the Golgi complex.Mechanisms of protein retention in the Golgi.Signaling circuits on the Golgi complex.Secretory protein biogenesis and traffic in the early secretory pathway The ArfGAP protein MoGlo3 regulates the development and pathogenicity of Magnaporthe oryzae.Arf1p provides an unexpected link between COPI vesicles and mRNA in Saccharomyces cerevisiae.Interaction of SNAREs with ArfGAPs precedes recruitment of Sec18p/NSF.ArfGAP1 responds to membrane curvature through the folding of a lipid packing sensor motif.Golgin160 recruits the dynein motor to position the Golgi apparatus Conserved molecular mechanisms underlying homeostasis of the Golgi complex.Dysregulated Arl1, a regulator of post-Golgi vesicle tethering, can inhibit endosomal transport and cell proliferation in yeast.Recruitment of Arf1-GDP to Golgi by Glo3p-type ArfGAPs is crucial for golgi maintenance and plant growth.Arf regulates interaction of GGA with mannose-6-phosphate receptor.

P2860

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P2860

ARF-GAP-mediated interaction between the ER-Golgi v-SNAREs and the COPI coat.

http://www.wikidata.org/entity/Q42917503

description

2002 nî lūn-bûn

@nan

2002年の論文

@ja

2002年論文

@yue

2002年論文

@zh-hant

2002年論文

@zh-hk

2002年論文

@zh-mo

2002年論文

@zh-tw

2002年论文

@wuu

2002年论文

@zh

2002年论文

@zh-cn

name

ARF-GAP-mediated interaction between the ER-Golgi v-SNAREs and the COPI coat.

@en

ARF-GAP-mediated interaction between the ER-Golgi v-SNAREs and the COPI coat.

@nl

type

label

ARF-GAP-mediated interaction between the ER-Golgi v-SNAREs and the COPI coat.

@en

ARF-GAP-mediated interaction between the ER-Golgi v-SNAREs and the COPI coat.

@nl

prefLabel

ARF-GAP-mediated interaction between the ER-Golgi v-SNAREs and the COPI coat.

@en

ARF-GAP-mediated interaction between the ER-Golgi v-SNAREs and the COPI coat.

@nl

P1433

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P1433

Journal of Cell Biology

P1476

ARF-GAP-mediated interaction between the ER-Golgi v-SNAREs and the COPI coat.

@en

P2093

Hans Dieter Schmitt

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

Rainer Duden

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

Ulrike Rein

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

Uwe Andag

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

P2860

Sec24 proteins and sorting at the endoplasmic reticulum

The KDEL receptor, ERD2, regulates intracellular traffic by recruiting a GTPase-activating protein for ARF1

COP I domains required for coatomer integrity, and novel interactions with ARF and ARF-GAP

Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 A resolution

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

Retrograde transport from the yeast Golgi is mediated by two ARF GAP proteins with overlapping function.

Three v-SNAREs and two t-SNAREs, present in a pentameric cis-SNARE complex on isolated vacuoles, are essential for homotypic fusion.

Reconstitution of retrograde transport from the Golgi to the ER in vitro.

SEC21 is a gene required for ER to Golgi protein transport that encodes a subunit of a yeast coatomer.

Identification of the catalytic domains and their functionally critical arginine residues of two yeast GTPase-activating proteins specific for Ypt/Rab transport GTPases

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395-404

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10.1083/JCB.200112092

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3

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157

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11970962

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2173288

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