Requirement for a GTPase-activating protein in vesicle budding from the endoplasmic reticulum.
about
p125 is a novel mammalian Sec23p-interacting protein with structural similarity to phospholipid-modifying proteinsMammalian homologues of yeast sec31p. An ubiquitously expressed form is localized to endoplasmic reticulum (ER) exit sites and is essential for ER-Golgi transportThe Ca2+-binding protein ALG-2 is recruited to endoplasmic reticulum exit sites by Sec31A and stabilizes the localization of Sec31ACloning and functional characterization of mammalian homologues of the COPII component Sec23Structural basis for cargo regulation of COPII coat assembly.Membrane recruitment of the cargo-selective retromer subcomplex is catalysed by the small GTPase Rab7 and inhibited by the Rab-GAP TBC1D5Diacylglycerol kinase delta suppresses ER-to-Golgi traffic via its SAM and PH domainsAssembly, organization, and function of the COPII coatInsights into COPII coat nucleation from the structure of Sec23.Sar1 complexed with the active fragment of Sec31An ACAP1-containing clathrin coat complex for endocytic recyclingIsolation and characterization of new Saccharomyces cerevisiae mutants perturbed in nuclear pore complex assemblyVesicle-mediated export from the ER: COPII coat function and regulationVesicle-mediated ER export of proteins and lipidsMolecular mechanisms of Sar/Arf GTPases in vesicular trafficking in yeast and plantsProtein export at the ER: loading big collagens into COPII carriersCellular COPII proteins are involved in production of the vesicles that form the poliovirus replication complex.Crystal structure of Sar1-GDP at 1.7 Å resolution and the role of the NH 2 terminus in ER exportStructure of the Sec23/24-Sar1 pre-budding complex of the COPII vesicle coatThe exomer cargo adaptor structure reveals a novel GTPase-binding domainThe exomer cargo adaptor features a flexible hinge domain.Sec16 influences transitional ER sites by regulating rather than organizing COPII.Sec23 homolog Nel1 is a novel GTPase-activating protein for Sar1 but does not function as a subunit of the coat protein complex II (COPII) coatYeast SEC16 gene encodes a multidomain vesicle coat protein that interacts with Sec23pSelective protein exit from yeast endoplasmic reticulum in absence of functional COPII coat component Sec13p.Sed4p stimulates Sar1p GTP hydrolysis and promotes limited coat disassembly.Smy2p participates in COPII vesicle formation through the interaction with Sec23p/Sec24p subcomplex.Evidence for separable functions of Srp1p, the yeast homolog of importin alpha (Karyopherin alpha): role for Srp1p and Sts1p in protein degradationThe Sec13p complex and reconstitution of vesicle budding from the ER with purified cytosolic 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.Proteomic analysis of nucleoporin interacting proteins.Traffic-independent function of the Sar1p/COPII machinery in proteasomal sorting of the cystic fibrosis transmembrane conductance regulatorSec16p potentiates the action of COPII proteins to bud transport vesiclesInsights into structural and regulatory roles of Sec16 in COPII vesicle formation at ER exit sites.Involvement of the penta-EF-hand protein Pef1p in the Ca2+-dependent regulation of COPII subunit assembly in Saccharomyces cerevisiae.SED4 encodes a yeast endoplasmic reticulum protein that binds Sec16p and participates in vesicle formation.Dynamics of the COPII coat with GTP and stable analogues.ATPase activity of a yeast secretory glycoprotein allows ER exit during inactivation of COPII components Sec24p and Sec13p.The Ypt1 GTPase is essential for the first two steps of the yeast secretory pathway.Dissection of COPII subunit-cargo assembly and disassembly kinetics during Sar1p-GTP hydrolysis.Cargo selection into COPII vesicles is driven by the Sec24p subunit.
P2860
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P2860
Requirement for a GTPase-activating protein in vesicle budding from the endoplasmic reticulum.
description
1993 nî lūn-bûn
@nan
1993 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
1993 թվականի մարտին հրատարակված գիտական հոդված
@hy
1993年の論文
@ja
1993年論文
@yue
1993年論文
@zh-hant
1993年論文
@zh-hk
1993年論文
@zh-mo
1993年論文
@zh-tw
1993年论文
@wuu
name
Requirement for a GTPase-activ ...... rom the endoplasmic reticulum.
@ast
Requirement for a GTPase-activ ...... rom the endoplasmic reticulum.
@en
Requirement for a GTPase-activ ...... rom the endoplasmic reticulum.
@nl
type
label
Requirement for a GTPase-activ ...... rom the endoplasmic reticulum.
@ast
Requirement for a GTPase-activ ...... rom the endoplasmic reticulum.
@en
Requirement for a GTPase-activ ...... rom the endoplasmic reticulum.
@nl
prefLabel
Requirement for a GTPase-activ ...... rom the endoplasmic reticulum.
@ast
Requirement for a GTPase-activ ...... rom the endoplasmic reticulum.
@en
Requirement for a GTPase-activ ...... rom the endoplasmic reticulum.
@nl
P3181
P356
P1433
P1476
Requirement for a GTPase-activ ...... rom the endoplasmic reticulum.
@en
P2093
T Yoshihisa
P304
P3181
P356
10.1126/SCIENCE.8451644
P407
P577
1993-03-05T00:00:00Z