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Opposing roles of Ubp3-dependent deubiquitination regulate replicative life span and heat resistance.
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Europe PubMed Central
PMC publication ID
4000091
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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:24596250%20AND%20SRC:MED&resulttype=core&format=json
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9 March 2020
title
Opposing roles of Ubp3-dependent deubiquitination regulate replicative life span and heat resistance
(English)
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PMC publication ID
4000091
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9 March 2020
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lifetime
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author
Kristian Kvint
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3
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4000091
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9 March 2020
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David Öling
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1
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4000091
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9 March 2020
Frederik Eisele
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2
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4000091
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9 March 2020
Thomas Nyström
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4
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9 March 2020
language of work or name
English
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4 March 2014
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4000091
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9 March 2020
published in
The EMBO Journal
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4000091
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9 March 2020
volume
33
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9 March 2020
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7
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9 March 2020
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747-761
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9 March 2020
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Enhancing protein disaggregation restores proteasome activity in aged cells
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Ras protein/cAMP-dependent protein kinase signaling is negatively regulated by a deubiquitinating enzyme, Ubp3, in yeast
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Molecular chaperones and stress-inducible protein-sorting factors coordinate the spatiotemporal distribution of protein aggregates
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Elevated proteasome capacity extends replicative lifespan in Saccharomyces cerevisiae
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Yeast deubiquitinase Ubp3 interacts with the 26 S proteasome to facilitate Rad4 degradation
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The mother enrichment program: a genetic system for facile replicative life span analysis in Saccharomyces cerevisiae
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Disruption of Rpn4-induced proteasome expression in Saccharomyces cerevisiae reduces cell viability under stressed conditions
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Misfolded proteins partition between two distinct quality control compartments
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Reversal of RNA polymerase II ubiquitylation by the ubiquitin protease Ubp3.
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Mature ribosomes are selectively degraded upon starvation by an autophagy pathway requiring the Ubp3p/Bre5p ubiquitin protease
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Atypical AAA+ subunit packing creates an expanded cavity for disaggregation by the protein-remodeling factor Hsp104.
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Accelerated aging and failure to segregate damaged proteins in Sir2 mutants can be suppressed by overproducing the protein aggregation-remodeling factor Hsp104p
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The cytoplasmic Hsp70 chaperone machinery subjects misfolded and endoplasmic reticulum import-incompetent proteins to degradation via the ubiquitin-proteasome system
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9 September 2017
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Rpn4 is a physiological substrate of the Ubr2 ubiquitin ligase
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9 September 2017
A versatile toolbox for PCR-based tagging of yeast genes: new fluorescent proteins, more markers and promoter substitution cassettes
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A genomic screen identifies Dsk2p and Rad23p as essential components of ER-associated degradation
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Ubp3 requires a cofactor, Bre5, to specifically de-ubiquitinate the COPII protein, Sec23.
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The yeast ubiquitin protease, Ubp3p, promotes protein stability
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A cryptic protease couples deubiquitination and degradation by the proteasome
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Ubiquitin-specific proteases of Saccharomyces cerevisiae. Cloning of UBP2 and UBP3, and functional analysis of the UBP gene family
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Rapid identification of yeast proteins on two-dimensional gels
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The Rsp5 ubiquitin ligase and the AAA-ATPase Cdc48 control the ubiquitin-mediated degradation of the COPII component Sec23.
1 reference
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reference URL
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The role of respiration, reactive oxygen species and oxidative stress in mother cell-specific ageing of yeast strains defective in the RAS signalling pathway
1 reference
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reference URL
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retrieved
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Use of two-dimensional gels in yeast proteomics
1 reference
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PubMed Central
reference URL
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1 reference
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reference URL
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1 reference
stated in
PubMed Central
reference URL
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retrieved
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Processing of proteins by the molecular chaperone Hsp104
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/24596250
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Transcriptional activation requires protection of the TATA-binding protein Tbp1 by the ubiquitin-specific protease Ubp3
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/24596250
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Use of CPY and its derivatives to study protein quality control in various cell compartments
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/24596250
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Identifiers
DOI
10.1002/EMBJ.201386822
1 reference
stated in
Europe PubMed Central
PMC publication ID
4000091
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:24596250%20AND%20SRC:MED&resulttype=core&format=json
retrieved
9 March 2020
PMC publication ID
4000091
1 reference
stated in
Europe PubMed Central
PMC publication ID
4000091
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:24596250%20AND%20SRC:MED&resulttype=core&format=json
retrieved
9 March 2020
PubMed publication ID
24596250
1 reference
stated in
Europe PubMed Central
PMC publication ID
4000091
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:24596250%20AND%20SRC:MED&resulttype=core&format=json
retrieved
9 March 2020
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