ArticlePloS one2013
Ubp2 regulates Rsp5 ubiquitination activity in vivo and in vitro.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 23 citations in OpenAlex.
- Environmental control of Pub1 (NEDD4 family E3 ligase) inLife science alliance · 2022Article
- α-Arrestins and Their Functions: From Yeast to Human Health.International journal of molecular sciences · 2022Review
- Deubiquitinating enzymes (DUBs): Regulation, homeostasis, and oxidative stress response.The Journal of biological chemistry · 2021Review
- Adaptors as the regulators of HECT ubiquitin ligases.Cell death and differentiation · 2021Review
- The structure and function of deubiquitinases: lessons from budding yeast.Open biology · 2020Review
- ESCRT-dependent protein sorting is required for the viability of yeast clathrin-mediated endocytosis mutants.Traffic (Copenhagen, Denmark) · 2020Article
- A Cycle of Ubiquitination Regulates Adaptor Function of the Nedd4-Family Ubiquitin Ligase Rsp5.Current biology : CB · 2020Article
- An ubiquitin-dependent balance between mitofusin turnover and fatty acids desaturation regulates mitochondrial fusion.Nature communications · 2017Article
- Deubiquitinase activity is required for the proteasomal degradation of misfolded cytosolic proteins upon heat-stress.Nature communications · 2016Article
- Role of Deubiquitinating Enzymes in DNA Repair.Molecular and cellular biology · 2016Review
- Review
- Guanine nucleotide-binding protein (Gα) endocytosis by a cascade of ubiquitin binding domain proteins is required for sustained morphogenesis and proper mating in yeast.The Journal of biological chemistry · 2014Article
- Quality control: quality control at the plasma membrane: one mechanism does not fit all.The Journal of cell biology · 2014Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The yeast HECT-family E3 ubiquitin ligase Rsp5 has been implicated in diverse cell functions. Previously, we and others [1], [2] reported the physical and functional interaction of Rsp5 with the deubiquitinating enzyme Ubp2, and the ubiquitin associated (UBA) domain-containing cofactor Rup1. To investigate the mechanism and significance of the Rsp5-Rup1-Ubp2 complex, we examined Rsp5 ubiquitination status in the presence or absence of these cofactors. We found that, similar to its mammalian homologues, Rsp5 is auto-ubiquitinated in vivo. Association with a substrate or Rup1 increased Rsp5 self-ubiquitination, whereas Ubp2 efficiently deubiquitinates Rsp5 in vivo and in vitro. The data reported here imply an auto-modulatory mechanism of Rsp5 regulation common to other E3 ligases.
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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.