The Emp24 complex recruits a specific cargo molecule into endoplasmic reticulum-derived vesicles
about
Proteomics of endoplasmic reticulum-Golgi intermediate compartment (ERGIC) membranes from brefeldin A-treated HepG2 cells identifies ERGIC-32, a new cycling protein that interacts with human Erv46The cargo receptors Surf4, endoplasmic reticulum-Golgi intermediate compartment (ERGIC)-53, and p25 are required to maintain the architecture of ERGIC and Golgi.Cell wall assembly in Saccharomyces cerevisiaeRole of Vma21p in assembly and transport of the yeast vacuolar ATPaseGolgi matrix proteins interact with p24 cargo receptors and aid their efficient retention in the Golgi apparatusThe GOLD domain, a novel protein module involved in Golgi function and secretionMolecular mechanisms of the localization of membrane proteins in the yeast Golgi compartmentsVesicle-mediated ER export of proteins and lipidsSelective protein exit from yeast endoplasmic reticulum in absence of functional COPII coat component Sec13p.ER cargo properties specify a requirement for COPII coat rigidity mediated by Sec13p.C26-CoA-dependent ceramide synthesis of Saccharomyces cerevisiae is operated by Lag1p and Lac1pGolgi-mediated glycosylation determines residency of the T2 RNase Rny1p in Saccharomyces cerevisiae.Suppression of coatomer mutants by a new protein family with COPI and COPII binding motifs in Saccharomyces cerevisiae.Oligomerization of a cargo receptor directs protein sorting into COPII-coated transport vesiclesInositol deacylation of glycosylphosphatidylinositol-anchored proteins is mediated by mammalian PGAP1 and yeast Bst1p.Immunoisolaton of the yeast Golgi subcompartments and characterization of a novel membrane protein, Svp26, discovered in the Sed5-containing compartments.Pga1 is an essential component of Glycosylphosphatidylinositol-mannosyltransferase II of Saccharomyces cerevisiae.Limited ER quality control for GPI-anchored proteins.Genomewide analysis reveals novel pathways affecting endoplasmic reticulum homeostasis, protein modification and quality control.GPI7 involved in glycosylphosphatidylinositol biosynthesis is essential for yeast cell separation.ATPase activity of a yeast secretory glycoprotein allows ER exit during inactivation of COPII components Sec24p and Sec13p.Ethanolaminephosphate side chain added to glycosylphosphatidylinositol (GPI) anchor by mcd4p is required for ceramide remodeling and forward transport of GPI proteins from endoplasmic reticulum to Golgi.Lst1p and Sec24p cooperate in sorting of the plasma membrane ATPase into COPII vesicles in Saccharomyces cerevisiae.Distinct retrieval and retention mechanisms are required for the quality control of endoplasmic reticulum protein folding.Secretory bulk flow of soluble proteins is efficient and COPII dependentGPI anchoring leads to sphingolipid-dependent retention of endocytosed proteins in the recycling endosomal compartment.Localization of p24 putative cargo receptors in the early secretory pathway depends on the biosynthetic activity of the cellPGAP2 is essential for correct processing and stable expression of GPI-anchored proteinsThe identification of a novel endoplasmic reticulum to Golgi SNARE complex used by the prechylomicron transport vesicleThe trafficking protein Tmed2/p24beta(1) is required for morphogenesis of the mouse embryo and placentaLectins and traffic in the secretory pathwayFunction of a p24 Heterodimer in Morphogenesis and Protein Transport in Penicillium oxalicumSorting of GPI-anchored proteins into ER exit sites by p24 proteins is dependent on remodeled GPIBiogenesis of tubular ER-to-Golgi transport intermediates.Quantitative ER <--> Golgi transport kinetics and protein separation upon Golgi exit revealed by vesicular integral membrane protein 36 dynamics in live cells.Disparate effects of p24alpha and p24delta on secretory protein transport and processing.Cytoplasmic accumulation of incompletely glycosylated SHBG enhances androgen action in proximal tubule epithelial cellsThe α-helical region in p24γ2 subunit of p24 protein cargo receptor is pivotal for the recognition and transport of glycosylphosphatidylinositol-anchored proteins.Erv14p directs a transmembrane secretory protein into COPII-coated transport vesicles.Biosynthesis of GPI-anchored proteins: special emphasis on GPI lipid remodeling.
P2860
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P2860
The Emp24 complex recruits a specific cargo molecule into endoplasmic reticulum-derived vesicles
description
2000 nî lūn-bûn
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name
The Emp24 complex recruits a s ...... mic reticulum-derived vesicles
@ast
The Emp24 complex recruits a s ...... mic reticulum-derived vesicles
@en
type
label
The Emp24 complex recruits a s ...... mic reticulum-derived vesicles
@ast
The Emp24 complex recruits a s ...... mic reticulum-derived vesicles
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prefLabel
The Emp24 complex recruits a s ...... mic reticulum-derived vesicles
@ast
The Emp24 complex recruits a s ...... mic reticulum-derived vesicles
@en
P2093
P2860
P356
P1476
The Emp24 complex recruits a s ...... mic reticulum-derived vesicles
@en
P2093
P2860
P304
P356
10.1083/JCB.148.5.925
P407
P577
2000-03-01T00:00:00Z