Autoubiquitination of the Hrd1 Ligase Triggers Protein Retrotranslocation in ERAD. (Q27935283)

PubMed publication ID

27321670

1 December 2016

title

Autoubiquitination of the Hrd1 Ligase Triggers Protein Retrotranslocation in ERAD. (English)

1 reference

PubMed publication ID

27321670

E3 ubiquitin-protein ligase HRD1 YOL013C

1 December 2016

main subject

1 reference

GOA release 2020-03-11

2

Tom A Rapoport

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author name string

Ryan D Baldridge

series ordinal

1

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language of work or name

English

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publication date

14 July 2016

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1 reference

PubMed publication ID

27321670

Channel crossing: how are proteins shipped across the bacterial plasma membrane?

1 December 2016

volume

166

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issue

2

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page(s)

394-407

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cites work

1 reference

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20 March 2017

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Key steps in ERAD of luminal ER proteins reconstituted with purified components

20 March 2017

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Der1 promotes movement of misfolded proteins through the endoplasmic reticulum membrane

20 March 2017

1 reference

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Ubiquitylation of an ERAD substrate occurs on multiple types of amino acids

20 March 2017

1 reference

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Retrotranslocation of a misfolded luminal ER protein by the ubiquitin-ligase Hrd1p

20 March 2017

1 reference

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Usa1 functions as a scaffold of the HRD-ubiquitin ligase.

20 March 2017

1 reference

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Sec61p is part of the endoplasmic reticulum-associated degradation machinery

20 March 2017

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Ubiquitination of serine, threonine, or lysine residues on the cytoplasmic tail can induce ERAD of MHC-I by viral E3 ligase mK3

20 March 2017

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Distinct ubiquitin-ligase complexes define convergent pathways for the degradation of ER proteins

20 March 2017

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A luminal surveillance complex that selects misfolded glycoproteins for ER-associated degradation

20 March 2017

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TEB4 is a C4HC3 RING finger-containing ubiquitin ligase of the endoplasmic reticulum

20 March 2017

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Distinct machinery is required in Saccharomyces cerevisiae for the endoplasmic reticulum-associated degradation of a multispanning membrane protein and a soluble luminal protein

20 March 2017

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A membrane protein complex mediates retro-translocation from the ER lumen into the cytosol

20 March 2017

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20 March 2017

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Misfolded proteins are sorted by a sequential checkpoint mechanism of ER quality control

20 March 2017

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Protein dislocation from the ER requires polyubiquitination and the AAA-ATPase Cdc48.

20 March 2017

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AAA-ATPase p97/Cdc48p, a cytosolic chaperone required for endoplasmic reticulum-associated protein degradation

20 March 2017

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The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol

20 March 2017

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HRD4/NPL4 is required for the proteasomal processing of ubiquitinated ER proteins

20 March 2017

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Distinct retrieval and retention mechanisms are required for the quality control of endoplasmic reticulum protein folding

20 March 2017

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Molecular chaperones in the yeast endoplasmic reticulum maintain the solubility of proteins for retrotranslocation and degradation

20 March 2017

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Functional domains of the Rsp5 ubiquitin-protein ligase.

20 March 2017

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Sec61p mediates export of a misfolded secretory protein from the endoplasmic reticulum to the cytosol for degradation

20 March 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4946995

Sec61-mediated transfer of a membrane protein from the endoplasmic reticulum to the proteasome for destruction

20 March 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4946995

Der1, a novel protein specifically required for endoplasmic reticulum degradation in yeast

20 March 2017

1 reference

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Cleaning up in the endoplasmic reticulum: ubiquitin in charge

20 March 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4946995

Protein quality control at the inner nuclear membrane

20 March 2017

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Sequential actions of the AAA-ATPase valosin-containing protein (VCP)/p97 and the proteasome 19 S regulatory particle in sterol-accelerated, endoplasmic reticulum (ER)-associated degradation of 3-hydroxy-3-methylglutaryl-coenzyme A reductase.

29 September 2017

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Decoupling the role of ubiquitination for the dislocation versus degradation of major histocompatibility complex (MHC) class I proteins during endoplasmic reticulum-associated degradation (ERAD)

29 September 2017

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Mechanisms of Sec61/SecY-mediated protein translocation across membranes

29 September 2017

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Ubiquitination of E3 ligases: self-regulation of the ubiquitin system via proteolytic and non-proteolytic mechanisms

29 September 2017

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The E3 ubiquitin ligases Hrd1 and gp78 bind to and promote cholera toxin retro-translocation

29 September 2017

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Sec61p is required for ERAD-L: genetic dissection of the translocation and ERAD-L functions of Sec61P using novel derivatives of CPY.

29 September 2017

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Sortagging: a versatile method for protein labeling

29 September 2017

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Ubiquitination of MHC class I heavy chains is essential for dislocation by human cytomegalovirus-encoded US2 but not US11.

29 September 2017

1 reference

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Protein translocation across biological membranes

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4946995

Ubiquitination on nonlysine residues by a viral E3 ubiquitin ligase

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4946995

Role of ubiquitination in retro-translocation of cholera toxin and escape of cytosolic degradation

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4946995

Endoplasmic reticulum degradation requires lumen to cytosol signaling. Transmembrane control of Hrd1p by Hrd3p.

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4946995

Sequence determinants for regulated degradation of yeast 3-hydroxy-3-methylglutaryl-CoA reductase, an integral endoplasmic reticulum membrane protein

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4946995

Evidence for the loop model of signal-sequence insertion into the endoplasmic reticulum

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4946995

The role of multiubiquitination in dislocation and degradation of the alpha subunit of the T cell antigen receptor

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4946995

A complex of Yos9p and the HRD ligase integrates endoplasmic reticulum quality control into the degradation machinery.

2 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4946995

Use of modular substrates demonstrates mechanistic diversity and reveals differences in chaperone requirement of ERAD.

27 November 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4946995

The Polycomb Protein Ring1B Generates Self Atypical Mixed Ubiquitin Chains Required for Its In Vitro Histone H2A Ligase Activity

27 November 2018

1 reference

https://pubmed.ncbi.nlm.nih.gov/27321670

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

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

https://pubmed.ncbi.nlm.nih.gov/27321670

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Analysis of two mutated vacuolar proteins reveals a degradation pathway in the endoplasmic reticulum or a related compartment of yeast

1 reference

https://pubmed.ncbi.nlm.nih.gov/27321670