GGA proteins bind ubiquitin to facilitate sorting at the trans-Golgi network.
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E3 ubiquitin ligase activity of the trifunctional ARD1 (ADP-ribosylation factor domain protein 1)VHS domains of ESCRT-0 cooperate in high-avidity binding to polyubiquitinated cargoUbiquitylation of leptin receptor OB-Ra regulates its clathrin-mediated endocytosisCrystal structure of human GGA1 GAT domain complexed with the GAT-binding domain of Rabaptin5Transport of LAPTM5 to lysosomes requires association with the ubiquitin ligase Nedd4, but not LAPTM5 ubiquitinationThe trans-Golgi network-associated human ubiquitin-protein ligase POSH is essential for HIV type 1 productionNeuronal precursor cell-expressed developmentally down-regulated 4-1 (NEDD4-1) controls the sorting of newly synthesized Ca(V)1.2 calcium channelsThe ESCRT machinery: from the plasma membrane to endosomes and back againThe Vps27/Hse1 Complex Is a GAT Domain-Based Scaffold for Ubiquitin-Dependent SortingGga2 mediates sequential ubiquitin-independent and ubiquitin-dependent steps in the trafficking of ARN1 from the trans-Golgi network to the vacuole.Lsb5p interacts with actin regulators Sla1p and Las17p, ubiquitin and Arf3p to couple actin dynamics to membrane trafficking processesGGA2- and ubiquitin-dependent trafficking of Arn1, the ferrichrome transporter of Saccharomyces cerevisiaeThe clathrin adaptor Gga2p is a phosphatidylinositol 4-phosphate effector at the Golgi exit.The Road not Taken: Less Traveled Roads from the TGN to the Plasma MembraneCinderella story: PI4P goes from precursor to key signaling moleculeUbiquitin-binding domainsUbiquitin-binding domainsHse1, a component of the yeast Hrs-STAM ubiquitin-sorting complex, associates with ubiquitin peptidases and a ligase to control sorting efficiency into multivesicular bodiesFunctional characterization of protein-sorting machineries at the trans-Golgi network in Drosophila melanogasterYarrowia lipolytica vesicle-mediated protein transport pathways.Structural basis for recognition of ubiquitinated cargo by Tom1-GAT domain.Defects in cellular sorting and retroviral assembly induced by GGA overexpressionQuantitative proteomics analysis of cell cycle-regulated Golgi disassembly and reassemblyManganese-induced trafficking and turnover of the cis-Golgi glycoprotein GPP130.Structural mechanism for ubiquitinated-cargo recognition by the Golgi-localized, gamma-ear-containing, ADP-ribosylation-factor-binding proteins.Golgi-to-late endosome trafficking of the yeast pheromone processing enzyme Ste13p is regulated by a phosphorylation site in its cytosolic domainUbiquitin regulates GGA3-mediated degradation of BACE1The GAT domains of clathrin-associated GGA proteins have two ubiquitin binding motifsEpidermal growth factor-dependent phosphorylation of the GGA3 adaptor protein regulates its recruitment to membranes.Stabilin-1 localizes to endosomes and the trans-Golgi network in human macrophages and interacts with GGA adaptors.Ubiquitin initiates sorting of Golgi and plasma membrane proteins into the vacuolar degradation pathway.Sorting signals that mediate traffic of chitin synthase III between the TGN/endosomes and to the plasma membrane in yeast.pH-dependent cargo sorting from the Golgi.Amino acids regulate retrieval of the yeast general amino acid permease from the vacuolar targeting pathway.Distinct roles for TGN/endosome epsin-like adaptors Ent3p and Ent5p.Insulin-regulated trafficking of GLUT4 requires ubiquitinationA single ubiquitin is sufficient for cargo protein entry into MVBs in the absence of ESCRT ubiquitinationThe Golgi-Localized γ-Ear-Containing ARF-Binding (GGA) Proteins Alter Amyloid-β Precursor Protein (APP) Processing through Interaction of Their GAE Domain with the Beta-Site APP Cleaving Enzyme 1 (BACE1)Ent3p and Ent5p exhibit cargo-specific functions in trafficking proteins between the trans-Golgi network and the endosomes in yeast.PI4P promotes the recruitment of the GGA adaptor proteins to the trans-Golgi network and regulates their recognition of the ubiquitin sorting signal
P2860
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P248
Q24293302-C0B3AB10-03E4-4335-BCA2-22AC9FDE2F14Q24299091-B7EB74C0-CB30-41D0-ACC9-D192C92FBA54Q24304963-BFCBE708-280A-41C3-BD88-FD9D4C1A10B7Q24305884-1314D601-757B-474F-80FB-BEF2C29D3BA9Q24318243-CFA3BAE2-01E4-4059-BED1-67D108C22C49Q24557498-120F7328-CCB6-4823-A1D3-9C16694BD27DQ24595139-9FE3E482-BD5E-429B-8092-5EC901927D22Q26849199-D587544D-4C54-4A15-99FB-274A6AC49416Q27645148-2563B4A5-423A-4D48-BA79-B385977A84A0Q27929961-CE07C092-1329-4732-BB07-B0033BDA6A5CQ27929982-A5BFFB92-FFDA-41D8-A2DB-5EC0476761BCQ27932123-3D7658ED-B10A-4848-A687-69BF7A94CFCDQ27933973-BCEC4231-1EF8-4831-92F5-88F8DBBCE937Q28082121-14EE1D6D-A753-4DE0-82C0-27695BA8B464Q28301748-186ADCA5-095C-4F7E-AB10-72B467C401DCQ29614358-D9C44DFE-183A-4C6F-896A-6FBD71AF6F32Q29616461-F1D2F4AF-E21A-4BED-A825-62816AA62E60Q30159582-8DD0D7A4-19A7-4F9A-8766-A9D7C4B8F999Q30492987-FF7E03C9-278F-4964-A8C6-32A67A0DEE2EQ30838050-2303612C-11DF-4018-90DE-AD971E800419Q33292326-AC4059EA-FCCA-4BE8-8DFA-212749B1E1C6Q33507450-0F602468-62EE-424E-9814-37C80A0F123EQ33522513-4666D5CB-0874-45A2-8E52-DB34FC0A7814Q33761520-74303980-3642-483D-8705-361C9179E780Q33850685-23057FA9-2516-4EE2-9F3B-8CD25D28598DQ33914482-E85185AC-3607-4102-AF89-EE3B67378328Q34025306-E2FF8A7F-550A-466A-B907-063362072CC1Q34026517-88A9EA22-0081-47C4-A281-5F33A71B0D9BQ34042776-EAD1C42A-871D-40DF-B445-55467516645AQ34345581-3E8B2708-8944-4419-8495-B3C2566CB858Q34412974-F5E562C4-7E83-46E5-AF37-040A3B024A93Q34441393-45684FBB-3A11-4CFA-876B-B1C275C5E5B1Q34695491-CAD36437-6CA9-4BFB-957D-D5ECFD2D9DB2Q34698090-5921FDCA-3A46-4CE0-B7FF-F9F65C7DA011Q35110770-752C276F-727C-4A1D-A4D2-6C9510E94DDEQ35153097-95B0B53D-4298-4C62-B102-4706B2742D28Q35210801-628CB6BF-2338-49D6-ACFF-72A7F753ADA9Q35656834-8620494C-2B81-4EB7-B8A1-DDEA36CF7AC3Q35757387-164128A8-08D4-408C-82DF-3FC89BDBA626Q35901860-957B699F-70EF-4E95-8C99-AE57C8D71BE5
P2860
GGA proteins bind ubiquitin to facilitate sorting at the trans-Golgi network.
description
2004 nî lūn-bûn
@nan
2004 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի մարտին հրատարակված գիտական հոդված
@hy
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
name
GGA proteins bind ubiquitin to facilitate sorting at the trans-Golgi network.
@ast
GGA proteins bind ubiquitin to facilitate sorting at the trans-Golgi network.
@en
GGA proteins bind ubiquitin to facilitate sorting at the trans-Golgi network.
@nl
type
label
GGA proteins bind ubiquitin to facilitate sorting at the trans-Golgi network.
@ast
GGA proteins bind ubiquitin to facilitate sorting at the trans-Golgi network.
@en
GGA proteins bind ubiquitin to facilitate sorting at the trans-Golgi network.
@nl
prefLabel
GGA proteins bind ubiquitin to facilitate sorting at the trans-Golgi network.
@ast
GGA proteins bind ubiquitin to facilitate sorting at the trans-Golgi network.
@en
GGA proteins bind ubiquitin to facilitate sorting at the trans-Golgi network.
@nl
P2093
P2860
P3181
P356
P1433
P1476
GGA proteins bind ubiquitin to facilitate sorting at the trans-Golgi network.
@en
P2093
Andrew D Robertson
Annette L Boman
Margaret M Allaman
Melissa J Hauglund
Olga Zhdankina
Patricia M Scott
Patricia S Bilodeau
Robert C Piper
Stanley C Winistorfer
William R Kearney
P2860
P2888
P3181
P356
10.1038/NCB1107
P407
P577
2004-03-01T00:00:00Z
P5875
P6179
1023876147