Localization of large ADP-ribosylation factor-guanine nucleotide exchange factors to different Golgi compartments: evidence for distinct functions in protein traffic
about
BIG1, a brefeldin A-inhibited guanine nucleotide-exchange protein, is required for correct glycosylation and function of integrin beta1Interaction of BIG2, a brefeldin A-inhibited guanine nucleotide-exchange protein, with exocyst protein Exo70Mon2, a relative of large Arf exchange factors, recruits Dop1 to the Golgi apparatusEffects of brefeldin A-inhibited guanine nucleotide-exchange (BIG) 1 and KANK1 proteins on cell polarity and directed migration during wound healingAMY-1 (associate of Myc-1) localization to the trans-Golgi network through interacting with BIG2, a guanine-nucleotide exchange factor for ADP-ribosylation factorsGBF1, a guanine nucleotide exchange factor for ADP-ribosylation factors, is localized to the cis-Golgi and involved in membrane association of the COPI coatADP-ribosylation factor/COPI-dependent events at the endoplasmic reticulum-Golgi interface are regulated by the guanine nucleotide exchange factor GBF1Specific functions of BIG1 and BIG2 in endomembrane organizationThe Sec7 guanine nucleotide exchange factor GBF1 regulates membrane recruitment of BIG1 and BIG2 guanine nucleotide exchange factors to the trans-Golgi network (TGN)Interaction of brefeldin A-inhibited guanine nucleotide-exchange protein (BIG) 1 and kinesin motor protein KIF21AA COPI coat subunit interacts directly with an early-Golgi localized Arf exchange factorThe membrane-tethering protein p115 interacts with GBF1, an ARF guanine-nucleotide-exchange factor.Dynamics of GBF1, a Brefeldin A-sensitive Arf1 exchange factor at the GolgiPhylogenetic analysis of Sec7-domain-containing Arf nucleotide exchangersAssembly, organization, and function of the COPII coatRab1b interacts with GBF1 and modulates both ARF1 dynamics and COPI association.Targeting of Arf-1 to the early Golgi by membrin, an ER-Golgi SNAREThe domain architecture of large guanine nucleotide exchange factors for the small GTP-binding protein ArfRegulation of small GTPases by GEFs, GAPs, and GDIsRegulating the large Sec7 ARF guanine nucleotide exchange factors: the when, where and how of activationCOPI budding within the Golgi stackThe ArfGEF GBF-1 Is Required for ER Structure, Secretion and Endocytic Transport in C. elegansThe capping domain in RalF regulates effector functionsChlamydia trachomatis co-opts GBF1 and CERT to acquire host sphingomyelin for distinct roles during intracellular developmentMouse Hepatitis Coronavirus RNA Replication Depends on GBF1-Mediated ARF1 ActivationGamma-COP appendage domain - structure and functionStructural Basis and Mechanism of Autoregulation in 3-Phosphoinositide-Dependent Grp1 Family Arf GTPase Exchange FactorsThe GTPase Arf1p and the ER to Golgi cargo receptor Erv14p cooperate to recruit the golgin Rud3p to the cis-Golgi.A novel Golgi membrane protein is a partner of the ARF exchange factors Gea1p and Gea2p.Mutations in a highly conserved region of the Arf1p activator GEA2 block anterograde Golgi transport but not COPI recruitment to membranes.Dissection of membrane dynamics of the ARF-guanine nucleotide exchange factor GBF1Hepatitis C virus triggers Golgi fragmentation and autophagy through the immunity-related GTPase M.Rab4 orchestrates a small GTPase cascade for recruitment of adaptor proteins to early endosomes.The Arf6 GEF GEP100/BRAG2 regulates cell adhesion by controlling endocytosis of beta1 integrins.Regulation of Arf activation: the Sec7 family of guanine nucleotide exchange factors.The yeast GRASP Grh1 colocalizes with COPII and is dispensable for organizing the secretory pathway.Unfolded protein response and cell death after depletion of brefeldin A-inhibited guanine nucleotide-exchange protein GBF1Modulation of cell adhesion and migration by the histone methyltransferase subunit mDpy-30 and its interacting proteins.Conserved oligomeric Golgi complex specifically regulates the maintenance of Golgi glycosylation machinery.Arf3 is activated uniquely at the trans-Golgi network by brefeldin A-inhibited guanine nucleotide exchange factors
P2860
Q24293210-04CBD149-8C5C-4C6C-AB37-FAB5580589DDQ24294708-0826FC8F-BC4D-4526-BDE4-65D28E4908DEQ24296460-3C0CB465-6858-4602-8B88-C138E3A717F2Q24297352-E49CB9B2-CBB0-4E11-B792-999EF90F6B7CQ24298016-6858BBC8-2F56-4F61-BF54-7F523E60FAC4Q24298818-68AACD6F-43C7-4496-A4F8-67D8FA25F7E5Q24305198-EDDCA01A-3F95-4736-8F39-E5B6912CDC09Q24305411-C6AC5AF0-8CF2-4D3B-A7A0-C9FEC1CBAC53Q24314741-A78A58F0-2154-498C-AD89-427FC42D3DA5Q24316191-DAC0ED38-A0A0-4708-AAAC-9D533416A6E5Q24318976-2181E4C6-09B9-4A68-9A43-847E9CA6FF06Q24534602-4FA01C7E-89C5-4EDD-83AC-A8EE47C824B1Q24556576-BF22A7F5-8D30-4D4A-A0F1-B3436AEBB8B4Q24610396-2B2A0A62-A6F1-49C0-A1CA-6FE983724C2AQ24655263-BDA137CE-55EC-4A75-9BE0-651D120D0EA3Q24670064-9E2EE3A2-8C1F-4FA6-9482-4A8B2119125DQ24678419-C88E5ECA-23A5-49DB-8AD0-75C8C20BFB4FQ24799194-DC998355-88E8-494E-810A-30D6A40D4A54Q26825750-87005F5A-0915-47B1-AE73-C8194394574CQ26827528-C8BF0394-8080-4E2B-BC0A-306251247C81Q27021670-19D5F4DD-5E9B-42AD-A193-A1B679381FD9Q27312637-9F8C5A7D-0ECD-4772-8A2C-C2FC16226E9BQ27340198-6FBE9E77-6963-4096-8B33-D7B83C276702Q27349136-43C5360D-1C40-4C0E-A6AD-BCDFB6965CD1Q27486170-21AD32AB-6A96-43F3-925A-68708C7264FEQ27642838-012771E1-E2DD-4617-B55E-0BD1E6657DD4Q27649147-69F39E28-7E03-45EC-BFD0-815DEDCC833CQ27934182-E2BC1F84-934E-4DA8-A73B-9E5F75983932Q27934502-9D6EC497-7787-4F6D-B111-8A9518B125C9Q27939138-642ED0E9-FB60-479C-9210-F756550B139FQ28243731-F8E4EA1E-8E4B-4CE2-82A6-39D48FD4DC43Q29871458-554A686D-A3E5-44C3-AD08-DD9A936E63C3Q30389378-45310C09-8BD1-4667-895A-EFB722A08710Q30421860-6679DD19-B321-459D-AC91-9532EBA9B056Q30444535-E9061C40-EF8C-419E-A9AA-844952A6DC0AQ30495976-C25EC176-20A7-4BCC-B81F-93D7316669B4Q33320586-4605A68B-C8BA-4ECB-A0D9-20EC031943E0Q33644584-D25D9683-C1F3-4F45-B24D-D908F63F4BEAQ33851058-CAC7534C-A051-44F0-8770-BC1B0DFD0B92Q33881671-8DF067F7-10FD-43D6-A64D-443DB48CB689
P2860
Localization of large ADP-ribosylation factor-guanine nucleotide exchange factors to different Golgi compartments: evidence for distinct functions in protein traffic
description
2002 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի հունվարին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 2002
@ast
im Januar 2002 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 2002/01/01)
@sk
vědecký článek publikovaný v roce 2002
@cs
wetenschappelijk artikel (gepubliceerd op 2002/01/01)
@nl
наукова стаття, опублікована в січні 2002
@uk
مقالة علمية (نشرت عام 2002)
@ar
name
Localization of large ADP-ribo ...... t functions in protein traffic
@ast
Localization of large ADP-ribo ...... t functions in protein traffic
@en
Localization of large ADP-ribo ...... t functions in protein traffic
@nl
type
label
Localization of large ADP-ribo ...... t functions in protein traffic
@ast
Localization of large ADP-ribo ...... t functions in protein traffic
@en
Localization of large ADP-ribo ...... t functions in protein traffic
@nl
prefLabel
Localization of large ADP-ribo ...... t functions in protein traffic
@ast
Localization of large ADP-ribo ...... t functions in protein traffic
@en
Localization of large ADP-ribo ...... t functions in protein traffic
@nl
P2860
P3181
P356
P1476
Localization of large ADP-ribo ...... t functions in protein traffic
@en
P2093
Troy K R Lasell
Xinhua Zhao
P2860
P304
P3181
P356
10.1091/MBC.01-08-0420
P577
2002-01-01T00:00:00Z