gp25L/emp24/p24 protein family members of the cis-Golgi network bind both COP I and II coatomer
about
Sec24 proteins and sorting at the endoplasmic reticulumLocalization and recycling of gp27 (hp24gamma3): complex formation with other p24 family membersProteomics 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 Erv46Syntaxin 17 cycles between the ER and ERGIC and is required to maintain the architecture of ERGIC and GolgiOligomeric state and stoichiometry of p24 proteins in the early secretory pathwayThe cargo receptors Surf4, endoplasmic reticulum-Golgi intermediate compartment (ERGIC)-53, and p25 are required to maintain the architecture of ERGIC and Golgi.Scyl1, mutated in a recessive form of spinocerebellar neurodegeneration, regulates COPI-mediated retrograde trafficProteinase-activated receptors, nucleotide P2Y receptors, and μ-opioid receptor-1B are under the control of the type I transmembrane proteins p23 and p24A in post-Golgi traffickingp24A, a type I transmembrane protein, controls ARF1-dependent resensitization of protease-activated receptor-2 by influence on receptor traffickingRecruitment to Golgi membranes of ADP-ribosylation factor 1 is mediated by the cytoplasmic domain of p23High-content screening microscopy identifies novel proteins with a putative role in secretory membrane trafficTyrosine phosphorylation of p97 regulates transitional endoplasmic reticulum assembly in vitroFunctional reconstitution of COPI coat assembly and disassembly using chemically defined componentsA single binding site for dilysine retrieval motifs and p23 within the gamma subunit of coatomerGolgi 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 secretionExpression, sorting, and segregation of Golgi proteins during germ cell differentiation in the testis.Scyl1 regulates Golgi morphologyThe transmembrane domain of hepatitis C virus glycoprotein E1 is a signal for static retention in the endoplasmic reticulum.Receptor-induced polymerization of coatomerAn acidic sequence of a putative yeast Golgi membrane protein binds COPII and facilitates ER export.Erp1p and Erp2p, partners for Emp24p and Erv25p in a yeast p24 complexSuppression of coatomer mutants by a new protein family with COPI and COPII binding motifs in Saccharomyces cerevisiae.Transport of axl2p depends on erv14p, an ER-vesicle protein related to the Drosophila cornichon gene product.ATPase activity of a yeast secretory glycoprotein allows ER exit during inactivation of COPII components Sec24p and Sec13p.Lst1p and Sec24p cooperate in sorting of the plasma membrane ATPase into COPII vesicles in Saccharomyces cerevisiae.Sec24p and Iss1p function interchangeably in transport vesicle formation from the endoplasmic reticulum in Saccharomyces cerevisiae.A comparative study of rat and human Tmp21 (p23) reveals the pseudogene-like features of human Tmp21-IIp24 and p23, the major transmembrane proteins of COPI-coated transport vesicles, form hetero-oligomeric complexes and cycle between the organelles of the early secretory pathwayGTP-dependent binding of ADP-ribosylation factor to coatomer in close proximity to the binding site for dilysine retrieval motifs and p23A sequence motif responsible for ER export and surface expression of Kir2.0 inward rectifier K(+) channelsCytosolic phospholipase A2-alpha associates with plasma membrane, endoplasmic reticulum and nuclear membrane in glomerular epithelial cellsLocalization of p24 putative cargo receptors in the early secretory pathway depends on the biosynthetic activity of the cellThe trafficking protein Tmed2/p24beta(1) is required for morphogenesis of the mouse embryo and placentaRab6 coordinates a novel Golgi to ER retrograde transport pathway in live cellsp24 proteins and quality control of LIN-12 and GLP-1 trafficking in Caenorhabditis elegansFunction of a p24 Heterodimer in Morphogenesis and Protein Transport in Penicillium oxalicumBiogenesis of tubular ER-to-Golgi transport intermediates.COPII-Golgi protein interactions regulate COPII coat assembly and Golgi size.Quantitative ER <--> Golgi transport kinetics and protein separation upon Golgi exit revealed by vesicular integral membrane protein 36 dynamics in live cells.
P2860
Q22009018-BD65A193-AB5D-487E-BB13-DD744E667CF9Q22009946-86A90749-D041-49BF-AF4B-1D3254AAE8F0Q24301091-3FE3DC78-E016-46E6-ACCF-4158894B0658Q24301490-BD183825-B3E0-472B-B57F-E2A728B5818BQ24306861-4C180509-7E1B-4D9A-B9EC-26681556FD37Q24315827-CE6F3576-418C-4650-B3D3-947CB0DF6F9BQ24321860-76AFAF44-C546-4778-AE9B-7FAA37A47014Q24336249-7FD10CFF-21A3-4371-B704-AC79F28B8F47Q24337278-AA0E8D27-9267-434B-A275-4A7D335BA2B8Q24534604-8ED922A4-CD14-4467-A985-7559E9C77E1DQ24562231-A6FF6F3E-CC8A-435C-8ACC-8EE7DD446F1FQ24676902-3E928D19-AC7F-4661-A4C1-ED31DD1917EDQ24680116-60D35B7D-B210-4AF4-825F-750B75DD617EQ24680266-01EB9897-C53F-449B-9FC4-A4130A741FE9Q24685223-1441CCD3-FC0B-4CF8-9345-39A0FEB1DA25Q24793827-50212005-469E-430C-8FCA-B6DB27C078F6Q27306405-07F200C7-9EA9-4428-BC26-06AE84E3A156Q27333695-D03B56E4-2B2F-4BB4-8E1F-D3A60C2679FEQ27469349-D544CACA-9EED-41D8-975C-2407B3B2465DQ27766896-817A61A4-0635-4F64-9464-EEC4772B20D6Q27934064-10028D61-6FB7-4DAE-A13A-5DD8F9CECF31Q27934318-57CB96EC-F6B3-42F5-9539-54E9E39D4B09Q27934758-944507DF-D752-4065-86C6-6EED17C7D7ADQ27935749-A189B178-F44D-4E84-B750-68723B7FF684Q27939316-3C1B11F1-8A31-476E-9AE5-04F360CD61ECQ27939936-C4E719B6-E0B9-46F0-B716-ACA244D6E4E8Q27940030-0DF48826-0DD0-4DD8-AB31-5E85CE35D6F0Q28137816-067BD75A-0FA7-49EA-AED1-B102DCFF6E55Q28142237-F9F2F8CD-C754-48AC-8FCD-4CB5EB382E8DQ28143515-E686C9EA-8E5C-42FD-AE48-4EA472444FB3Q28210516-8170165C-864F-4D3C-AE38-7E44645639F2Q28345075-FB94937E-89BA-4494-A76A-445589F624F6Q28364638-B1158FC7-62A6-41C0-8F4B-C9A429ACE088Q28589953-AB6343B0-FF6F-45CA-A1F4-A972B83649A2Q28609753-688CB8F6-390D-42FF-A792-112C858C6765Q28619405-7F1B6601-00B1-46A5-B22F-958B575687F8Q28647453-073E4ED0-87E0-466E-AB38-583B0D3BC1AEQ30476699-5B2ABCD4-BCBC-4305-9061-0E1B90E7ACD3Q30480431-5C66DF43-B9E1-496F-9664-4B167B645E96Q30525331-CF5092A1-EB66-489A-9412-351E4BDEEDE2
P2860
gp25L/emp24/p24 protein family members of the cis-Golgi network bind both COP I and II coatomer
description
1998 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 1998
@ast
im Februar 1998 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 1998/02/23)
@sk
vědecký článek publikovaný v roce 1998
@cs
wetenschappelijk artikel (gepubliceerd op 1998/02/23)
@nl
наукова стаття, опублікована в лютому 1998
@uk
مقالة علمية (نشرت في 23-2-1998)
@ar
name
gp25L/emp24/p24 protein family ...... ind both COP I and II coatomer
@ast
gp25L/emp24/p24 protein family ...... ind both COP I and II coatomer
@en
gp25L/emp24/p24 protein family ...... ind both COP I and II coatomer
@nl
type
label
gp25L/emp24/p24 protein family ...... ind both COP I and II coatomer
@ast
gp25L/emp24/p24 protein family ...... ind both COP I and II coatomer
@en
gp25L/emp24/p24 protein family ...... ind both COP I and II coatomer
@nl
prefLabel
gp25L/emp24/p24 protein family ...... ind both COP I and II coatomer
@ast
gp25L/emp24/p24 protein family ...... ind both COP I and II coatomer
@en
gp25L/emp24/p24 protein family ...... ind both COP I and II coatomer
@nl
P2093
P2860
P356
P1476
gp25L/emp24/p24 protein family ...... ind both COP I and II coatomer
@en
P2093
J Füllekrug
J J Bergeron
J P Paccaud
K Dejgaard
M Dominguez
P2860
P304
P356
10.1083/JCB.140.4.751
P407
P577
1998-02-01T00:00:00Z