A transmembrane ubiquitin ligase required to sort membrane proteins into multivesicular bodies.
about
The FAM deubiquitylating enzyme localizes to multiple points of protein trafficking in epithelia, where it associates with E-cadherin and beta-cateninMisfolding diverts CFTR from recycling to degradation: quality control at early endosomesThe C2 domain of the Rsp5 ubiquitin ligase binds membrane phosphoinositides and directs ubiquitination of endosomal cargoLoss of Vac14, a regulator of the signaling lipid phosphatidylinositol 3,5-bisphosphate, results in neurodegeneration in mice.Selective destruction of abnormal proteins by ubiquitin-mediated protein quality control degradationProtein homeostasis at the plasma membraneGGA2- and ubiquitin-dependent trafficking of Arn1, the ferrichrome transporter of Saccharomyces cerevisiaeRetrograde transport of the mannosyltransferase Och1p to the early Golgi requires a component of the COG transport complex.Intravacuolar membrane lysis in Saccharomyces cerevisiae. Does vacuolar targeting of Cvt17/Aut5p affect its function?Direct binding to Rsp5p regulates ubiquitination-independent vacuolar transport of Sna3p.DOA1/UFD3 plays a role in sorting ubiquitinated membrane proteins into multivesicular bodiesTransferrin receptor-like proteins control the degradation of a yeast metal transporterKei1: a novel subunit of inositolphosphorylceramide synthase, essential for its enzyme activity and Golgi localization.Multivesicular body sorting: ubiquitin ligase Rsp5 is required for the modification and sorting of carboxypeptidase S.Direct binding to Rsp5 mediates ubiquitin-independent sorting of Sna3 via the multivesicular body pathway.Ergosterol is required for targeting of tryptophan permease to the yeast plasma membrane.Bsd2 binds the ubiquitin ligase Rsp5 and mediates the ubiquitination of transmembrane proteins.Swf1-dependent palmitoylation of the SNARE Tlg1 prevents its ubiquitination and degradationHse1, a component of the yeast Hrs-STAM ubiquitin-sorting complex, associates with ubiquitin peptidases and a ligase to control sorting efficiency into multivesicular bodiesInefficient quality control of thermosensitive proteins on the plasma membraneRobustness and evolvability in natural chemical resistance: identification of novel systems properties, biochemical mechanisms and regulatory interactions.Ubiquitin-mediated targeting of a mutant plasma membrane ATPase, Pma1-7, to the endosomal/vacuolar system in yeastEvasion of endoplasmic reticulum surveillance makes Wsc1p an obligate substrate of Golgi quality controlQuality control for unfolded proteins at the plasma membrane.Recognition and ubiquitination of Salmonella type III effector SopA by a ubiquitin E3 ligase, HsRMA1.Downregulation of cell surface receptors by the K3 family of viral and cellular ubiquitin E3 ligases.Identification of candidate substrates for the Golgi Tul1 E3 ligase using quantitative diGly proteomics in yeast.Yeast SREBP cleavage activation requires the Golgi Dsc E3 ligase complex.Secretory pathway quality control operating in Golgi, plasmalemmal, and endosomal systems.Role of calnexin in the glycan-independent quality control of proteolipid protein.Routing misfolded proteins through the multivesicular body (MVB) pathway protects against proteotoxicity.Yeast sterol regulatory element-binding protein (SREBP) cleavage requires Cdc48 and Dsc5, a ubiquitin regulatory X domain-containing subunit of the Golgi Dsc E3 ligaseDirect sorting of the yeast uracil permease to the endosomal system is controlled by uracil binding and Rsp5p-dependent ubiquitylation.E3 ligases in T cell anergy--turning immune responses into tolerance.Endoplasmic Reticulum Exit of Golgi-resident Defective for SREBP Cleavage (Dsc) E3 Ligase Complex Requires Its ActivityThe transmembrane domain of acid trehalase mediates ubiquitin-independent multivesicular body pathway sortingMembrane-anchored ubiquitin ligase complex is required for the turnover of lysosomal membrane proteins.Targeting of Sna3p to the endosomal pathway depends on its interaction with Rsp5p and multivesicular body sorting on its ubiquitylationInduced oligomerization targets Golgi proteins for degradation in lysosomes.Enzyme reversal to explore the function of yeast E3 ubiquitin-ligases.
P2860
Q24610351-C8698475-0F8A-4230-A95E-21190304A947Q24676764-8F138140-C41F-4865-B151-9C817872808FQ24677536-99434337-655E-48BB-8670-1B94E3F60798Q24678783-A4BA7667-9161-4656-8C69-1D0F180E2675Q26824733-2F36DAE9-FDEE-415D-9F97-AC6D1A53BF99Q27009009-A3F06D91-B8B7-4AD9-8F96-0957454BD1A9Q27932123-76DCB086-5139-4DB0-B307-F71E550FF8EFQ27932804-CB225163-7437-4672-82DE-0954FF2753BAQ27932809-D62C7159-27EF-4ECC-A5BB-DFB01111F5FBQ27933875-6FA239D1-7C89-4BA4-BAFA-95016B6787C1Q27934992-2CDD1BE8-8BA4-4B74-A934-B54531DC5729Q27935937-B91FF112-9D0C-4BDE-8D06-5ACB6248845CQ27937152-EF2176C8-5F46-490E-A6EB-3362B213DD6FQ27937366-BDCACBA7-06AF-4967-97AE-B0D35AC83C3EQ27937377-5D883BE7-8C3D-4EC5-BA2D-457229454689Q27937645-932EDE88-1A62-421A-A203-885CBCB92A41Q27939068-A4CC0927-3C8C-4886-8177-D22F7C2AD689Q27939433-E4F4A40D-11F3-4B1E-B9DF-202E73DEE4FFQ30159582-19D370A3-8B26-4266-9C85-9969F5002811Q33425200-1E81F5FF-0BEF-452C-891B-AC2A582D45C7Q33592328-6B1FD8C8-AAE2-4F8F-B729-78CAA2E2E94BQ33693280-FC1A9EF5-18AB-4253-9061-91DE7B109C86Q33761462-B0CA43A3-8395-4B13-A3B1-69D3E4FC5095Q34412404-FB5FF50A-258E-4D32-AEEA-C3A3A6279A79Q34452782-C40B2304-60BF-407C-A84A-7202DB108851Q34453408-DA787FAC-29FB-435F-9D30-9A232816BF2CQ34468295-846B0886-F538-462B-A234-81F251CC748CQ34874112-543A357D-09FB-4E8B-A32D-21923AA5C90FQ34970141-4D49963D-13C5-433D-8ACA-0465A56E10F6Q35107713-160027FD-ECA9-4EFC-A74F-9737CAF3B421Q35310258-9C6E69F3-F7D6-4B88-B3F3-817D083E7999Q35643838-5341B3BA-9F08-41F3-9E07-7F6AF8C2532DQ35803062-627E06FC-11B5-4ACF-84C7-40AC6CC973A0Q35835790-FBC15817-EC24-43B1-A433-8483B4C2307AQ35860773-626CA97C-08DC-490C-A062-3694BD53D2D6Q35901885-4A74F2A2-E8C8-46C0-89ED-9BEC700BEE59Q36266173-A8EFCBDF-1DC6-4FD8-950F-2E531A71FAE6Q36320200-62B6EC12-B512-4D0F-80D7-E69237E41D77Q36337034-F14253C4-506E-419D-931D-3F182A3418BEQ36337590-855C370A-5298-4223-AC3F-5F8F1E0DB0FC
P2860
A transmembrane ubiquitin ligase required to sort membrane proteins into multivesicular bodies.
description
2002 nî lūn-bûn
@nan
2002 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
name
A transmembrane ubiquitin liga ...... ns into multivesicular bodies.
@ast
A transmembrane ubiquitin liga ...... ns into multivesicular bodies.
@en
A transmembrane ubiquitin liga ...... ns into multivesicular bodies.
@nl
type
label
A transmembrane ubiquitin liga ...... ns into multivesicular bodies.
@ast
A transmembrane ubiquitin liga ...... ns into multivesicular bodies.
@en
A transmembrane ubiquitin liga ...... ns into multivesicular bodies.
@nl
prefLabel
A transmembrane ubiquitin liga ...... ns into multivesicular bodies.
@ast
A transmembrane ubiquitin liga ...... ns into multivesicular bodies.
@en
A transmembrane ubiquitin liga ...... ns into multivesicular bodies.
@nl
P2860
P356
P1433
P1476
A transmembrane ubiquitin liga ...... ns into multivesicular bodies.
@en
P2093
Hugh R B Pelham
P2860
P2888
P304
P356
10.1038/NCB743
P407
P577
2002-02-01T00:00:00Z
P5875
P6179
1000686957