The ESCRT-III subunit hVps24 is required for degradation but not silencing of the epidermal growth factor receptor.
about
Spongiform neurodegeneration-associated E3 ligase Mahogunin ubiquitylates TSG101 and regulates endosomal traffickingCHMP7, a novel ESCRT-III-related protein, associates with CHMP4b and functions in the endosomal sorting pathwayRin1 interacts with signal-transducing adaptor molecule (STAM) and mediates epidermal growth factor receptor trafficking and degradationHuman ESCRT-II complex and its role in human immunodeficiency virus type 1 releaseVps22/EAP30 in ESCRT-II mediates endosomal sorting of growth factor and chemokine receptors destined for lysosomal degradationBiogenesis and function of multivesicular bodiesESCRT-II coordinates the assembly of ESCRT-III filaments for cargo sorting and multivesicular body vesicle formationUbc4/5 and c-Cbl continue to ubiquitinate EGF receptor after internalization to facilitate polyubiquitination and degradationNo strings attached: the ESCRT machinery in viral budding and cytokinesisSCAMP3 negatively regulates epidermal growth factor receptor degradation and promotes receptor recycling.Fab1 phosphatidylinositol 3-phosphate 5-kinase controls trafficking but not silencing of endocytosed receptorsRelease of autoinhibition converts ESCRT-III components into potent inhibitors of HIV-1 buddingStructural insight into the ESCRT-I/-II link and its role in MVB traffickingThe role of the endosomal sorting complexes required for transport (ESCRT) in tumorigenesisEndosome maturationALIX and ESCRT-I/II function as parallel ESCRT-III recruiters in cytokinetic abscission.Spastin and ESCRT-III coordinate mitotic spindle disassembly and nuclear envelope sealingSpg20-/- mice reveal multimodal functions for Troyer syndrome protein spartin in lipid droplet maintenance, cytokinesis and BMP signalingEndocytosis and signalling: intertwining molecular networksTargeting of AMSH to endosomes is required for epidermal growth factor receptor degradation.Essential role of ubiquitin and TSG101 protein in formation and function of the central supramolecular activation cluster.Loss of function of the ALS protein SigR1 leads to ER pathology associated with defective autophagy and lipid raft disturbancesGenetic interactions between the Drosophila tumor suppressor gene ept and the stat92E transcription factor.Disruption of endocytic trafficking in frontotemporal dementia with CHMP2B mutations.The basic amino acids in the coiled-coil domain of CIN85 regulate its interaction with c-Cbl and phosphatidic acid during epidermal growth factor receptor (EGFR) endocytosis.Old world arenaviruses enter the host cell via the multivesicular body and depend on the endosomal sorting complex required for transportMolecular Mechanisms that Regulate Epidermal Growth Factor Receptor InactivationBiogenesis of lysosome-related organelles complex-1 subunit 1 (BLOS1) interacts with sorting nexin 2 and the endosomal sorting complex required for transport-I (ESCRT-I) component TSG101 to mediate the sorting of epidermal growth factor receptor intGLUT4 traffic through an ESCRT-III-dependent sorting compartment in adipocytes.Endocytosis and intracellular trafficking of ErbBs.The ocular albinism type 1 (OA1) GPCR is ubiquitinated and its traffic requires endosomal sorting complex responsible for transport (ESCRT) functionRouting misfolded proteins through the multivesicular body (MVB) pathway protects against proteotoxicity.Drosophila Vps4 promotes Epidermal growth factor receptor signaling independently of its role in receptor degradation.Endosomal accumulation of the activated epidermal growth factor receptor (EGFR) induces apoptosisIdentification of an AAA ATPase VPS4B-dependent pathway that modulates epidermal growth factor receptor abundance and signaling during hypoxia.Seven-transmembrane receptors and ubiquitinationComparative Analysis of Transmembrane Regulators of the Filamentous Growth Mitogen-Activated Protein Kinase Pathway Uncovers Functional and Regulatory DifferencesEndocytic control of growth factor signalling: multivesicular bodies as signalling organellesFunctional multivesicular bodies are required for autophagic clearance of protein aggregates associated with neurodegenerative disease.Late endosomal traffic of the epidermal growth factor receptor ensures spatial and temporal fidelity of mitogen-activated protein kinase signaling
P2860
Q24293322-096983C9-97C1-4EF7-9330-C7E004130C59Q24297581-73723A5A-99E2-4828-A572-74114737E742Q24301513-0DEE0FF5-FED6-417E-9007-C94C5F7D4ABFQ24303183-165A0941-00EC-4881-B21E-4CAD152856B7Q24338164-1854F2D3-2870-41DE-97C5-38C2347D22F5Q24601502-C8A79234-8336-4A74-9191-F91784AAA665Q24629620-604A79D9-963B-45A9-86D7-F87A3C6E37A6Q24653688-F9C9041A-64F4-4CD3-9911-D894E1125CACQ24655056-7C1C429B-22C8-4C60-8203-5A3075BF9029Q24657896-FFA2162C-06DE-4B17-B465-6FDC6D5DA6A6Q24671705-47602C0C-3AD3-4E0F-A454-0FC64EFBDCF5Q24677985-D55E34E1-0802-4361-B507-0A9D2C0E909AQ24682152-7C89142F-EBD2-4C4A-A558-CE421905A1A9Q26864942-93281683-C6E4-4D18-A0ED-9DC831B75AD1Q26992067-F7910D3A-D005-43BE-A500-AB344E582E06Q27309069-E4B3EEC2-6669-4AFA-93EB-90212AD06979Q28117647-95180C7B-55EB-4994-B833-064C3DB7859FQ28511369-4F17FE43-CBC0-4761-8742-D52D3ABD09FEQ29616848-565CBA64-F480-4FFB-B100-4F997580B84BQ30159469-30EA4D91-D9FC-4802-93D1-A92903150A46Q30495533-23D92938-6AAD-4E71-8CC8-22E8000852B0Q30669509-640E4D30-6729-48F5-AE47-0EED494BC355Q33507271-8480B13F-71E0-4B53-9732-1C054AC354EBQ33832871-4FE31FF3-3EA8-4CA8-8637-2B8EB3E1531CQ33895325-0CBFC0B4-4DC6-4E95-87E2-3ADF316B2C31Q34023003-D520C736-E856-4CF9-ADCE-73BC41652E9BQ34213559-C36E7B73-D943-49D1-A491-8BAF41372C09Q34355752-EC223DA1-52D3-49FD-97D6-254833E35F62Q34437868-8BAD031B-6757-43A9-AA62-4333882C665AQ34827744-B36B0E0D-68CC-43A7-852C-C17A063EB620Q35123182-11D6D261-8E4B-4565-A114-EEA634F950E4Q35310258-8785F8D4-6750-4C1C-A00F-DD9A0B689BB3Q35355864-A71C3B6E-DD6B-4628-BB8A-C6E8FB0294FDQ35643854-140CE715-FD2B-4EF6-8634-6405BACF79A4Q35806672-987D48C4-F8ED-4FDF-AFFC-2C77052C6A02Q35951259-81E51BBC-415F-4684-B3D5-49D9C55466A3Q36001598-8B50F8CA-56AD-463C-A65B-BDAA9E7CE1D1Q36029933-751014F0-87CA-4680-9951-E757CE25B300Q36119653-81CB9F3D-0020-4D70-8A66-4773F6D95B23Q36173900-189776EE-4CA0-4EAD-B6C5-9AEE76F28FE3
P2860
The ESCRT-III subunit hVps24 is required for degradation but not silencing of the epidermal growth factor receptor.
description
2006 nî lūn-bûn
@nan
2006 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի մարտին հրատարակված գիտական հոդված
@hy
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
name
The ESCRT-III subunit hVps24 i ...... idermal growth factor receptor
@nl
The ESCRT-III subunit hVps24 i ...... dermal growth factor receptor.
@ast
The ESCRT-III subunit hVps24 i ...... dermal growth factor receptor.
@en
type
label
The ESCRT-III subunit hVps24 i ...... idermal growth factor receptor
@nl
The ESCRT-III subunit hVps24 i ...... dermal growth factor receptor.
@ast
The ESCRT-III subunit hVps24 i ...... dermal growth factor receptor.
@en
prefLabel
The ESCRT-III subunit hVps24 i ...... idermal growth factor receptor
@nl
The ESCRT-III subunit hVps24 i ...... dermal growth factor receptor.
@ast
The ESCRT-III subunit hVps24 i ...... dermal growth factor receptor.
@en
P2093
P2860
P50
P921
P356
P1476
The ESCRT-III subunit hVps24 i ...... idermal growth factor receptor
@en
P2093
Andreas Brech
Camilla Raiborg
Delphine Lechardeur
Kristi G Bache
Lene Malerød
Susanne Stuffers
Thomas Slagsvold
P2860
P304
P356
10.1091/MBC.E05-10-0915
P407
P577
2006-03-22T00:00:00Z