The Hrd1p ligase complex forms a linchpin between ER-lumenal substrate selection and Cdc48p recruitment
about
SEL1L protein critically determines the stability of the HRD1-SEL1L endoplasmic reticulum-associated degradation (ERAD) complex to optimize the degradation kinetics of ERAD substratesSynoviolin promotes IRE1 ubiquitination and degradation in synovial fibroblasts from mice with collagen-induced arthritisRNF185 is a novel E3 ligase of endoplasmic reticulum-associated degradation (ERAD) that targets cystic fibrosis transmembrane conductance regulator (CFTR)Folding-competent and folding-defective forms of ricin A chain have different fates after retrotranslocation from the endoplasmic reticulumOne step at a time: endoplasmic reticulum-associated degradationRecent technical developments in the study of ER-associated degradationEndoplasmic reticulum-mediated protein quality control in ArabidopsisSelective destruction of abnormal proteins by ubiquitin-mediated protein quality control degradationMechanisms for quality control of misfolded transmembrane proteinsRoad to ruin: targeting proteins for degradation in the endoplasmic reticulumStructural and Biochemical Basis of Yos9 Protein Dimerization and Possible Contribution to Self-association of 3-Hydroxy-3-methylglutaryl-Coenzyme A Reductase Degradation Ubiquitin-Ligase ComplexRecognition of an ERAD-L substrate analyzed by site-specific in vivo photocrosslinking.Sec61p is part of the endoplasmic reticulum-associated degradation machineryDefining the glycan destruction signal for endoplasmic reticulum-associated degradationA Complex of Htm1 and the Oxidoreductase Pdi1 Accelerates Degradation of Misfolded Glycoproteins.Yos9p assists in the degradation of certain nonglycosylated proteins from the endoplasmic reticulumLimited ER quality control for GPI-anchored proteins.Der1 promotes movement of misfolded proteins through the endoplasmic reticulum membrane.Retrotranslocation of a misfolded luminal ER protein by the ubiquitin-ligase Hrd1p.Htm1 protein generates the N-glycan signal for glycoprotein degradation in the endoplasmic reticulumAssociation of the SEL1L protein transmembrane domain with HRD1 ubiquitin ligase regulates ERAD-LCleaning up in the endoplasmic reticulum: ubiquitin in chargeEmerging functions of the VCP/p97 AAA-ATPase in the ubiquitin systemCytosolic entry of Shiga-like toxin a chain from the yeast endoplasmic reticulum requires catalytically active Hrd1pUsa1 protein facilitates substrate ubiquitylation through two separate domainsStringent requirement for HRD1, SEL1L, and OS-9/XTP3-B for disposal of ERAD-LS substrates.Modularity of the Hrd1 ERAD complex underlies its diverse client range.The endoplasmic reticulum-associated degradation of the epithelial sodium channel requires a unique complement of molecular chaperones.A nucleus-based quality control mechanism for cytosolic proteinsQuality and quantity control at the endoplasmic reticulum.Misfolded proteins induce aggregation of the lectin Yos9.SPFH2 mediates the endoplasmic reticulum-associated degradation of inositol 1,4,5-trisphosphate receptors and other substrates in mammalian cells.Requirements for the selective degradation of CD4 receptor molecules by the human immunodeficiency virus type 1 Vpu protein in the endoplasmic reticulum.The interplay of Hrd3 and the molecular chaperone system ensures efficient degradation of malfolded secretory proteins.Proteostasis regulation at the endoplasmic reticulum: a new perturbation site for targeted cancer therapy.Yeast sterol regulatory element-binding protein (SREBP) cleavage requires Cdc48 and Dsc5, a ubiquitin regulatory X domain-containing subunit of the Golgi Dsc E3 ligaseRkr1/Ltn1 Ubiquitin Ligase-mediated Degradation of Translationally Stalled Endoplasmic Reticulum Proteins.Subcellular Fractionation Analysis of the Extraction of Ubiquitinated Polytopic Membrane Substrate during ER-Associated DegradationAberrant substrate engagement of the ER translocon triggers degradation by the Hrd1 ubiquitin ligase.SEL1L, the homologue of yeast Hrd3p, is involved in protein dislocation from the mammalian ER.
P2860
Q24298501-B7295B34-8518-4170-97EC-3B094211494FQ24314799-D2D357E9-12EF-44BD-AFE6-71DB492FEE3FQ24323658-5EC8463E-CB35-46AF-9106-6BF679971381Q24600792-7FC6207E-CA43-41AE-84DC-AF3C811CC3A2Q24658302-C5A416BA-34C6-46A9-80ED-9BF9CBEB6E8AQ26823514-5A7C9F98-F53E-4CF1-81FD-DF0E1912E384Q26824018-6F75BF72-3A77-47D7-B81C-F7D22A5866B4Q26824733-DEF09945-0C02-42A5-9678-87253F41CE99Q26830475-7A6C6C46-0E49-4FA9-B987-97622CE513B6Q26866096-568D3676-B215-4528-9DA6-ECAC8D5AA9D9Q27676812-570BCB7B-51BE-4969-9009-B1C63CB9640CQ27930293-0BF76BA8-F92E-45BE-9084-03C5973C51D7Q27930621-0626BC2E-F55F-44E3-A628-20FC74958B99Q27932810-DA652E52-926C-4A41-9B2C-372A5BDA3F53Q27935416-9E171267-5229-498D-BD47-0AE9AB7EBA60Q27936890-00AE44C4-6D1B-4C2F-ABB9-C7FC86C96EA3Q27937610-5741D6C1-93F3-4505-9761-0300FCBDAD0BQ27938831-5892B3B9-E524-4236-B93D-848A7C7CB63EQ27938951-0BA213C4-3E7D-4D5C-A09E-F173201AFBC8Q27939524-E7BFD965-F02C-4541-9EEF-B240E71A731CQ28119008-4FC4FAE7-C7F4-4839-B859-8338CEFE58C8Q28237362-B330800C-875D-4668-9503-FBBAA0EAC9A8Q28258706-692C2A3B-F99E-4E0D-90D4-4113C29371EBQ28481415-1ABE691F-30F2-4F23-BFE8-905AFA595FC6Q33515572-07B4ADF3-5DFD-4667-8834-E44BAE382F34Q33615098-E41A5DD1-CD50-4914-89DD-03518107A530Q33717057-0A47D197-1C0D-46A7-AEF6-60BFB55CB22CQ33721156-D7B6D933-4858-4AD0-9C5D-075AFB426EECQ33948472-677B1B4E-FA2C-404C-A3C6-F9FB549C947AQ34090425-578D2128-785D-4C95-A2AC-4EAE3CFEB28FQ34170723-5C6C51A7-A0EB-4DE0-8D2E-DC37D4D0BC3CQ34628253-ECF87321-8E31-4A1C-8D4A-E1708898FD46Q34701164-9F317E4F-698C-4076-A151-D031ECAAC6B2Q34960632-30A65DB1-A4EF-417B-A862-A4A9CB6D5180Q35469778-A777F6EE-54FC-4BC1-864B-22916C644FB4Q35643838-5F229B91-9884-45B7-AC99-C84637B4FD82Q35883810-14AC1113-ADAB-4780-A935-0FE7AA18D0B9Q35915784-23AA3EB4-9370-4EDD-8DB4-5CEC510FC14DQ36027390-1BDCE570-EBC7-40B4-B254-1D9C4AABDECFQ36119119-4ACF35D5-8B6C-435A-B2E0-A78C67A4E002
P2860
The Hrd1p ligase complex forms a linchpin between ER-lumenal substrate selection and Cdc48p recruitment
description
2006 nî lūn-bûn
@nan
2006 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի մայիսին 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 Hrd1p ligase complex forms ...... lection and Cdc48p recruitment
@ast
The Hrd1p ligase complex forms ...... lection and Cdc48p recruitment
@en
The Hrd1p ligase complex forms ...... ection and Cdc48p recruitment.
@nl
type
label
The Hrd1p ligase complex forms ...... lection and Cdc48p recruitment
@ast
The Hrd1p ligase complex forms ...... lection and Cdc48p recruitment
@en
The Hrd1p ligase complex forms ...... ection and Cdc48p recruitment.
@nl
prefLabel
The Hrd1p ligase complex forms ...... lection and Cdc48p recruitment
@ast
The Hrd1p ligase complex forms ...... lection and Cdc48p recruitment
@en
The Hrd1p ligase complex forms ...... ection and Cdc48p recruitment.
@nl
P2093
P2860
P3181
P356
P1433
P1476
The Hrd1p ligase complex forms ...... lection and Cdc48p recruitment
@en
P2093
Ernst Jarosch
Robert Gauss
Thomas Sommer
P2860
P304
P3181
P356
10.1038/SJ.EMBOJ.7601088
P407
P577
2006-05-03T00:00:00Z