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The Hrd1p ligase complex forms a linchpin between ER-lumenal substrate selection and Cdc48p recruitment
scientific article
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scholarly article
1 reference
stated in
PubMed
PubMed ID
16619026
retrieved
1 December 2016
title
The Hrd1p ligase complex forms a linchpin between ER-lumenal substrate selection and Cdc48p recruitment
(English)
1 reference
stated in
PubMed
PubMed ID
16619026
retrieved
1 December 2016
main subject
Hrd1p ubiquitin ligase complex
1 reference
stated in
Gene Ontology release 2020-05-02
Gene Ontology ID
GO:0000836
AAA family ATPase CDC48 YDL126C
1 reference
stated in
GOA release 2020-03-11
Derlin YBR201W
1 reference
stated in
GOA release 2020-03-11
Ubiquitin ligase complex subunit HRD3 YLR207W
1 reference
stated in
GOA release 2020-03-11
E3 ubiquitin-protein ligase HRD1 YOL013C
1 reference
stated in
GOA release 2020-03-11
Carboxypeptidase C PRC1 YMR297W
1 reference
stated in
GOA release 2020-03-11
author name string
Robert Gauss
series ordinal
1
0 references
Thomas Sommer
series ordinal
2
0 references
Ernst Jarosch
series ordinal
3
0 references
language of work or name
English
0 references
publication date
3 May 2006
0 references
published in
The EMBO Journal
1 reference
stated in
PubMed
PubMed ID
16619026
retrieved
1 December 2016
volume
25
0 references
page(s)
1827-35
0 references
issue
9
0 references
cites work
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Ubx2 links the Cdc48 complex to ER-associated protein degradation
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Membrane-bound Ubx2 recruits Cdc48 to ubiquitin ligases and their substrates to ensure efficient ER-associated protein degradation
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A membrane protein complex mediates retro-translocation from the ER lumen into the cytosol
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A membrane protein required for dislocation of misfolded proteins from the ER
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Human HRD1 is an E3 ubiquitin ligase involved in degradation of proteins from the endoplasmic reticulum
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Function of the p97-Ufd1-Npl4 complex in retrotranslocation from the ER to the cytosol: dual recognition of nonubiquitinated polypeptide segments and polyubiquitin chains
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AAA-ATPase p97/Cdc48p, a cytosolic chaperone required for endoplasmic reticulum-associated protein degradation
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The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol
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HRD4/NPL4 is required for the proteasomal processing of ubiquitinated ER proteins
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Mobilization of processed, membrane-tethered SPT23 transcription factor by CDC48(UFD1/NPL4), a ubiquitin-selective chaperone
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The tumor autocrine motility factor receptor, gp78, is a ubiquitin protein ligase implicated in degradation from the endoplasmic reticulum
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Involvement of valosin-containing protein, an ATPase Co-purified with IkappaBalpha and 26 S proteasome, in ubiquitin-proteasome-mediated degradation of IkappaBalpha
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Degradation of subunits of the Sec61p complex, an integral component of the ER membrane, by the ubiquitin-proteasome pathway.
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AAA ATPase p97/valosin-containing protein interacts with gp78, a ubiquitin ligase for endoplasmic reticulum-associated degradation
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1 reference
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reference URL
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29 September 2017
Role of the ubiquitin-selective CDC48(UFD1/NPL4 )chaperone (segregase) in ERAD of OLE1 and other substrates
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reference URL
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29 September 2017
Endoplasmic reticulum degradation requires lumen to cytosol signaling. Transmembrane control of Hrd1p by Hrd3p.
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stated in
PubMed Central
reference URL
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29 September 2017
Role of 26S proteasome and HRD genes in the degradation of 3-hydroxy-3-methylglutaryl-CoA reductase, an integral endoplasmic reticulum membrane protein
1 reference
stated in
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29 September 2017
New modules for the repeated internal and N-terminal epitope tagging of genes in Saccharomyces cerevisiae.
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27 November 2018
Vpu-mediated degradation of CD4 reconstituted in yeast reveals mechanistic differences to cellular ER-associated protein degradation
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27 November 2018
Cdc48p is required for the cell cycle commitment point at Start via degradation of the G1-CDK inhibitor Far1p
1 reference
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PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1456945
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27 November 2018
Use of modular substrates demonstrates mechanistic diversity and reveals differences in chaperone requirement of ERAD.
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27 November 2018
A Major Conformational Change in p97 AAA ATPase upon ATP Binding
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/16619026
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
A RING-H2 finger motif is essential for the function of Der3/Hrd1 in endoplasmic reticulum associated protein degradation in the yeast Saccharomyces cerevisiae
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/16619026
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Genetic interactions of Hrd3p and Der3p/Hrd1p with Sec61p suggest a retro-translocation complex mediating protein transport for ER degradation
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/16619026
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae
1 reference
stated in
Crossref
reference URL
https://api.crossref.org/works/10.1038%2FSJ.EMBOJ.7601088
retrieved
7 January 2021
based on heuristic
inferred from DOI database lookup
Identifiers
DOI
10.1038/SJ.EMBOJ.7601088
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
4804631
OpenCitations bibliographic resource ID
4804631
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
4804631
PMCID
1456945
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
4804631
PubMed ID
16619026
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
4804631
ResearchGate publication ID
7161270
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