Role of 26S proteasome and HRD genes in the degradation of 3-hydroxy-3-methylglutaryl-CoA reductase, an integral endoplasmic reticulum membrane protein.
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RING fingers mediate ubiquitin-conjugating enzyme (E2)-dependent ubiquitinationThe tumor autocrine motility factor receptor, gp78, is a ubiquitin protein ligase implicated in degradation from the endoplasmic reticulumA membrane protein required for dislocation of misfolded proteins from the ERDefining human ERAD networks through an integrative mapping strategySEL1L protein critically determines the stability of the HRD1-SEL1L endoplasmic reticulum-associated degradation (ERAD) complex to optimize the degradation kinetics of ERAD substratesHuman HRD1 is an E3 ubiquitin ligase involved in degradation of proteins from the endoplasmic reticulumWolfram syndrome 1 gene negatively regulates ER stress signaling in rodent and human cellsSterol-regulated degradation of Insig-1 mediated by the membrane-bound ubiquitin ligase gp78UBXD7 binds multiple ubiquitin ligases and implicates p97 in HIF1alpha turnoverSynoviolin promotes IRE1 ubiquitination and degradation in synovial fibroblasts from mice with collagen-induced arthritisMultiprotein complexes that link dislocation, ubiquitination, and extraction of misfolded proteins from the endoplasmic reticulum membrane.Proteins of the endoplasmic-reticulum-associated degradation pathway: domain detection and function predictionSEL1L affects human pancreatic cancer cell cycle and invasiveness through modulation of PTEN and genes related to cell-matrix interactionsCdc53/cullin and the essential Hrt1 RING-H2 subunit of SCF define a ubiquitin ligase module that activates the E2 enzyme Cdc34One step at a time: endoplasmic reticulum-associated degradationMisfolded proteins are sorted by a sequential checkpoint mechanism of ER quality controlA molecular portrait of the response to unfolded proteinsRheumatoid arthritis as a hyper-endoplasmic-reticulum-associated degradation diseaseCancer Microenvironment and Endoplasmic Reticulum Stress ResponseSelective destruction of abnormal proteins by ubiquitin-mediated protein quality control degradationUbiquitin ligases in cholesterol metabolismIn vivo action of the HRD ubiquitin ligase complex: mechanisms of endoplasmic reticulum quality control and sterol regulation.Previously unknown role for the ubiquitin ligase Ubr1 in endoplasmic reticulum-associated protein degradation.Recognition of an ERAD-L substrate analyzed by site-specific in vivo photocrosslinking.Sec61p mediates export of a misfolded secretory protein from the endoplasmic reticulum to the cytosol for degradation.Sec61p is part of the endoplasmic reticulum-associated degradation machineryA regulatory link between ER-associated protein degradation and the unfolded-protein response.The conserved npl4 protein complex mediates proteasome-dependent membrane-bound transcription factor activation.The protein translocation channel binds proteasomes to the endoplasmic reticulum membraneDeterminants of RING-E2 fidelity for Hrd1p, a membrane-anchored ubiquitin ligase.Quality control of inner nuclear membrane proteins by the Asi complex.The Hrd1p ligase complex forms a linchpin between ER-lumenal substrate selection and Cdc48p recruitmentMembrane topology and function of Der3/Hrd1p as a ubiquitin-protein ligase (E3) involved in endoplasmic reticulum degradation.Analysis of quality control substrates in distinct cellular compartments reveals a unique role for Rpn4p in tolerating misfolded membrane proteins.An HRD/DER-independent ER quality control mechanism involves Rsp5p-dependent ubiquitination and ER-Golgi transportSubcellular distribution of proteasomes implicates a major location of protein degradation in the nuclear envelope-ER network in yeast.Der3p/Hrd1p is required for endoplasmic reticulum-associated degradation of misfolded lumenal and integral membrane proteins.A proteasomal ATPase contributes to dislocation of endoplasmic reticulum-associated degradation (ERAD) substrates.Traffic-independent function of the Sar1p/COPII machinery in proteasomal sorting of the cystic fibrosis transmembrane conductance regulatorMembrane-bound Ubx2 recruits Cdc48 to ubiquitin ligases and their substrates to ensure efficient ER-associated protein degradation.
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P2860
Role of 26S proteasome and HRD genes in the degradation of 3-hydroxy-3-methylglutaryl-CoA reductase, an integral endoplasmic reticulum membrane protein.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on December 1996
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Role of 26S proteasome and HRD ...... ic reticulum membrane protein.
@en
Role of 26S proteasome and HRD ...... ic reticulum membrane protein.
@nl
type
label
Role of 26S proteasome and HRD ...... ic reticulum membrane protein.
@en
Role of 26S proteasome and HRD ...... ic reticulum membrane protein.
@nl
prefLabel
Role of 26S proteasome and HRD ...... ic reticulum membrane protein.
@en
Role of 26S proteasome and HRD ...... ic reticulum membrane protein.
@nl
P2093
P2860
P356
P1476
Role of 26S proteasome and HRD ...... ic reticulum membrane protein.
@en
P2093
P2860
P304
P356
10.1091/MBC.7.12.2029
P577
1996-12-01T00:00:00Z