ArticleMolecular biology of the cell1999
Interaction of the Doa4 deubiquitinating enzyme with the yeast 26S proteasome.
Article in Molecular biology of the cell, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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Who cites it
42 citing papers in PubMed, 123 citations in OpenAlex.
- Mechanisms and Design Principles of Proteolysis-Targeting Chimeras and Their Emerging Applications.ACS pharmacology & translational science · 2026Review
- Transcriptomic analysis reveals hub genes and pathways in response to acetic acid stress in Kluyveromyces marxianus during high-temperature ethanol fermentation.Stress biology · 2023Article
- The structure and function of deubiquitinases: lessons from budding yeast.Open biology · 2020Review
- Yeast Pah1p phosphatidate phosphatase is regulated by proteasome-mediated degradation.The Journal of biological chemistry · 2014Article
- Identification and proteomic analysis of distinct UBE3A/E6AP protein complexes.Molecular and cellular biology · 2012Article
- The prolific ATL family of RING-H2 ubiquitin ligases.Plant signaling & behavior · 2012Review
- Intersection of the multivesicular body pathway and lipid homeostasis in RNA replication by a positive-strand RNA virus.Journal of virology · 2011Article
- Yeast deubiquitinase Ubp3 interacts with the 26 S proteasome to facilitate Rad4 degradation.The Journal of biological chemistry · 2010Article
- Affinity purification strategy to capture human endogenous proteasome complexes diversity and to identify proteasome-interacting proteins.Molecular & cellular proteomics : MCP · 2009Article
- Transgenic rescue of ataxia mice reveals a male-specific sterility defect.Developmental biology · 2009Article
- Relative structural and functional roles of multiple deubiquitylating proteins associated with mammalian 26S proteasome.Molecular biology of the cell · 2008Article
- Molecular basis for bre5 cofactor recognition by the ubp3 deubiquitylating enzyme.Journal of molecular biology · 2007Article
- Dual mechanisms specify Doa4-mediated deubiquitination at multivesicular bodies.The EMBO journal · 2007Article
- Article
- A conserved late endosome-targeting signal required for Doa4 deubiquitylating enzyme function.The Journal of cell biology · 2006Article
- Genetic interactions of a putative Arabidopsis thaliana ubiquitin-ligase with components of the Saccharomyces cerevisiae ubiquitination machinery.Current genetics · 2006Article
- Distinct functional domains of Ubc9 dictate cell survival and resistance to genotoxic stress.Molecular and cellular biology · 2006Article
- Riding the DUBway: regulation of protein trafficking by deubiquitylating enzymes.The Journal of cell biology · 2006Review
- Structure and mechanisms of the proteasome-associated deubiquitinating enzyme USP14.The EMBO journal · 2005Article
- Proteasomal ATPase-associated factor 1 negatively regulates proteasome activity by interacting with proteasomal ATPases.Molecular and cellular biology · 2005Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
e Saccharomyces cerevisiae Doa4 deubiquitinating enzyme is required for the rapid degradation of protein substrates of the ubiquitin-proteasome pathway. Previous work suggested that Doa4 functions late in the pathway, possibly by deubiquitinating (poly)-ubiquitin-substrate intermediates associated with the 26S proteasome. We now provide evidence for physical and functional interaction between Doa4 and the proteasome. Genetic interaction is indicated by the mutual enhancement of defects associated with a deletion of DOA4 or a proteasome mutation when the two mutations are combined. Physical association of Doa4 and the proteasome was investigated with a new yeast 26S proteasome purification procedure, by which we find that a sizeable fraction of Doa4 copurifies with the protease. Another yeast deubiquitinating enzyme, Ubp5, which is related in sequence to Doa4 but cannot substitute for it even when overproduced, does not associate with the proteasome. DOA4-UBP5 chimeras were made by a novel PCR/yeast recombination method and used to identify an N-terminal 310-residue domain of Doa4 that, when appended to the catalytic domain of Ubp5, conferred Doa4 function, consistent with Ubp enzymes having a modular architecture. Unlike Ubp5, a functional Doa4-Ubp5 chimera associates with the proteasome, suggesting that proteasome binding is important for Doa4 function. Together, these data support a model in which Doa4 promotes proteolysis through removal of ubiquitin from proteolytic intermediates on the proteasome before or after initiation of substrate breakdown.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.