Aberrant substrate engagement of the ER translocon triggers degradation by the Hrd1 ubiquitin ligase.
about
Futile protein folding cycles in the ER are terminated by the unfolded protein O-mannosylation pathway.The yeast ERAD-C ubiquitin ligase Doa10 recognizes an intramembrane degronN-terminal acetylation of the yeast Derlin Der1 is essential for Hrd1 ubiquitin-ligase activity toward luminal ER substrates.Yeast importin-α (Srp1) performs distinct roles in the import of nuclear proteins and in targeting proteasomes to the nucleus.Cleaning up in the endoplasmic reticulum: ubiquitin in chargeRab2A is a pivotal switch protein that promotes either secretion or ER-associated degradation of (pro)insulin in insulin-secreting cells.Degradation of specific nuclear proteins occurs in the cytoplasm in Saccharomyces cerevisiae.Ube2g2-gp78-mediated HERP polyubiquitylation is involved in ER stress recoveryGrowth-based determination and biochemical confirmation of genetic requirements for protein degradation in Saccharomyces cerevisiaeUbiquitin-dependent protein degradation at the yeast endoplasmic reticulum and nuclear envelope.Cotranslational stabilization of Sec62/63 within the ER Sec61 translocon is controlled by distinct substrate-driven translocation events.Rkr1/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 DegradationThe endoplasmic reticulum-associated degradation pathways of budding yeast.Cleaning up: ER-associated degradation to the rescue.The Protease Ste24 Clears Clogged TransloconsHsp70 targets a cytoplasmic quality control substrate to the San1p ubiquitin ligaseA Conserved C-terminal Element in the Yeast Doa10 and Human MARCH6 Ubiquitin Ligases Required for Selective Substrate Degradation.Cycloheximide Chase Analysis of Protein Degradation in Saccharomyces cerevisiaeThree old and one new: protein import into red algal-derived plastids surrounded by four membranes.Quality control: ER-associated degradation: protein quality control and beyondRegulation of Endoplasmic Reticulum-Associated Protein Degradation (ERAD) by Ubiquitin.Proteolytic regulation of metabolic enzymes by E3 ubiquitin ligase complexes: lessons from yeast.Acetylation of N-terminus and two internal amino acids is dispensable for degradation of a protein that aberrantly engages the endoplasmic reticulum translocon.Glycosylation-directed quality control of protein folding.The Sec63p J-domain is required for ERAD of soluble proteins in yeast.Diminished Ost3-dependent N-glycosylation of the BiP nucleotide exchange factor Sil1 is an adaptive response to reductive ER stress.Can modulators of apolipoproteinB biogenesis serve as an alternate target for cholesterol-lowering drugs?
P2860
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P2860
Aberrant substrate engagement of the ER translocon triggers degradation by the Hrd1 ubiquitin ligase.
description
2012 nî lūn-bûn
@nan
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
2012年论文
@zh
2012年论文
@zh-cn
name
Aberrant substrate engagement ...... by the Hrd1 ubiquitin ligase.
@ast
Aberrant substrate engagement ...... by the Hrd1 ubiquitin ligase.
@en
type
label
Aberrant substrate engagement ...... by the Hrd1 ubiquitin ligase.
@ast
Aberrant substrate engagement ...... by the Hrd1 ubiquitin ligase.
@en
prefLabel
Aberrant substrate engagement ...... by the Hrd1 ubiquitin ligase.
@ast
Aberrant substrate engagement ...... by the Hrd1 ubiquitin ligase.
@en
P2093
P2860
P356
P1476
Aberrant substrate engagement ...... n by the Hrd1 ubiquitin ligase
@en
P2093
Eric M Rubenstein
Robert Swanson
Stefan G Kreft
Wesley Greenblatt
P2860
P304
P356
10.1083/JCB.201203061
P407
P577
2012-06-01T00:00:00Z