A novel GTP-binding protein, Sar1p, is involved in transport from the endoplasmic reticulum to the Golgi apparatus.
about
Hypothetical protein KIAA0079 is a mammalian homologue of yeast Sec24pp125 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 Sec31AArf, Arl, Arp and Sar proteins: a family of GTP-binding proteins with a structural device for 'front-back' communication.Selective amplification of additional members of the ADP-ribosylation factor (ARF) family: cloning of additional human and Drosophila ARF-like genesRab1b regulates vesicular transport between the endoplasmic reticulum and successive Golgi compartmentsAssembly, organization, and function of the COPII coatHuman SEC13Rp functions in yeast and is located on transport vesicles budding from the endoplasmic reticulumCalexcitin: a signaling protein that binds calcium and GTP, inhibits potassium channels, and enhances membrane excitabilitySurrounding tissues canalize motile cardiopharyngeal progenitors towards collective polarity and directed migration.Crystal structure of Sar1-GDP at 1.7 Å resolution and the role of the NH 2 terminus in ER exportSec16 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 Sec23pCOPII subunit interactions in the assembly of the vesicle coat.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.Golgi structure correlates with transitional endoplasmic reticulum organization in Pichia pastoris and Saccharomyces cerevisiae.Cytosolic Sec13p complex is required for vesicle formation from the endoplasmic reticulum in vitro.Sed4p stimulates Sar1p GTP hydrolysis and promotes limited coat disassembly.Smy2p participates in COPII vesicle formation through the interaction with Sec23p/Sec24p subcomplex.The 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.Autophagosome requires specific early Sec proteins for its formation and NSF/SNARE for vacuolar fusionOligomerization of a cargo receptor directs protein sorting into COPII-coated transport vesiclesThe yeast SLY gene products, suppressors of defects in the essential GTP-binding Ypt1 protein, may act in endoplasmic reticulum-to-Golgi transportSec16p 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.The Saccharomyces cerevisiae SEC20 gene encodes a membrane glycoprotein which is sorted by the HDEL retrieval system.Bos1p, a membrane protein required for ER to Golgi transport in yeast, co-purifies with the carrier vesicles and with Bet1p and the ER membrane.Emp47p and its close homolog Emp46p have a tyrosine-containing endoplasmic reticulum exit signal and function in glycoprotein secretion in Saccharomyces cerevisiaeIdentification of Prp40, a novel essential yeast splicing factor associated with the U1 small nuclear ribonucleoprotein particleSED5 encodes a 39-kD integral membrane protein required for vesicular transport between the ER and the Golgi complex.SED4 encodes a yeast endoplasmic reticulum protein that binds Sec16p and participates in vesicle formation.Dissection of COPII subunit-cargo assembly and disassembly kinetics during Sar1p-GTP hydrolysis.Genes that control the fidelity of endoplasmic reticulum to Golgi transport identified as suppressors of vesicle budding mutations.Identification and structure of four yeast genes (SLY) that are able to suppress the functional loss of YPT1, a member of the RAS superfamily.Aut7p, a soluble autophagic factor, participates in multiple membrane trafficking processes.The TIP1 gene of Saccharomyces cerevisiae encodes an 80 kDa cytoplasmic protein that interacts with the cytoplasmic domain of Sec20pA link between secretion and pre-mRNA processing defects in Saccharomyces cerevisiae and the identification of a novel splicing gene, RSE1
P2860
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P2860
A novel GTP-binding protein, Sar1p, is involved in transport from the endoplasmic reticulum to the Golgi apparatus.
description
1989 nî lūn-bûn
@nan
1989年の論文
@ja
1989年論文
@yue
1989年論文
@zh-hant
1989年論文
@zh-hk
1989年論文
@zh-mo
1989年論文
@zh-tw
1989年论文
@wuu
1989年论文
@zh
1989年论文
@zh-cn
name
A novel GTP-binding protein, S ...... iculum to the Golgi apparatus.
@ast
A novel GTP-binding protein, S ...... iculum to the Golgi apparatus.
@en
type
label
A novel GTP-binding protein, S ...... iculum to the Golgi apparatus.
@ast
A novel GTP-binding protein, S ...... iculum to the Golgi apparatus.
@en
prefLabel
A novel GTP-binding protein, S ...... iculum to the Golgi apparatus.
@ast
A novel GTP-binding protein, S ...... iculum to the Golgi apparatus.
@en
P2860
P356
P1476
A novel GTP-binding protein, S ...... ticulum to the Golgi apparatus
@en
P2093
M Muramatsu
P2860
P304
P356
10.1083/JCB.109.6.2677
P407
P433
P577
1989-12-01T00:00:00Z