ArticleGenetics2001
WW domains of Rsp5p define different functions: determination of roles in fluid phase and uracil permease endocytosis in Saccharomyces cerevisiae.
Article in Genetics, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 58 citations in OpenAlex.
- Chaperone-Dependent Degradation of Cdc42 Promotes Cell Polarity and Shields the Protein from Aggregation.Molecular and cellular biology · 2023Article
- Regulation of Cdc42 protein turnover modulates the filamentous growth MAPK pathway.The Journal of cell biology · 2022Article
- A Cycle of Ubiquitination Regulates Adaptor Function of the Nedd4-Family Ubiquitin Ligase Rsp5.Current biology : CB · 2020Article
- Activity of a ubiquitin ligase adaptor is regulated by disordered insertions in its arrestin domain.Molecular biology of the cell · 2019Article
- USP9X Deubiquitylates DVL2 to Regulate WNT Pathway Specification.Cell reports · 2019Article
- Rsp5/Nedd4 is the main ubiquitin ligase that targets cytosolic misfolded proteins following heat stress.Nature cell biology · 2014Article
- Convergence of ubiquitylation and phosphorylation signaling in rapamycin-treated yeast cells.Molecular & cellular proteomics : MCP · 2014Article
- Regulation of clathrin-mediated endocytosis by dynamic ubiquitination and deubiquitination.Current biology : CB · 2014Article
- Article
- Rsp5 ubiquitin ligase is required for protein trafficking in Saccharomyces cerevisiae COPI mutants.PloS one · 2012Article
- Clathrin-mediated endocytosis in budding yeast.Trends in cell biology · 2012Review
- Yeast ubiquitin ligase Rsp5 contains nuclear localization and export signals.European journal of cell biology · 2011Article
- WW domains 2 and 3 of Rsp5p play overlapping roles in binding to the LPKY motif of Spt23p and Mga2p.The international journal of biochemistry & cell biology · 2008Article
- Targeting of Sna3p to the endosomal pathway depends on its interaction with Rsp5p and multivesicular body sorting on its ubiquitylation.Traffic (Copenhagen, Denmark) · 2007Article
- Direct binding to Rsp5p regulates ubiquitination-independent vacuolar transport of Sna3p.Molecular biology of the cell · 2007Article
- Characterization of multiple multivesicular body sorting determinants within Sna3: a role for the ubiquitin ligase Rsp5.Molecular biology of the cell · 2007Article
- Hse1, a component of the yeast Hrs-STAM ubiquitin-sorting complex, associates with ubiquitin peptidases and a ligase to control sorting efficiency into multivesicular bodies.Molecular biology of the cell · 2007Article
- Enhanced levels of Pis1p (phosphatidylinositol synthase) improve the growth of Saccharomyces cerevisiae cells deficient in Rsp5 ubiquitin ligase.The Biochemical journal · 2006Article
- Rsp5 ubiquitin ligase modulates translation accuracy in yeast Saccharomyces cerevisiae.RNA (New York, N.Y.) · 2005Article
- Novel interaction between Apc5p and Rsp5p in an intracellular signaling pathway in Saccharomyces cerevisiae.Eukaryotic cell · 2005Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Rsp5p, ubiquitin-protein ligase, an enzyme of the ubiquitination pathway, contains three WW domains that mediate protein-protein interactions. To determine if these domains adapt Rsp5p to a subset of substrates involved in numerous cellular processes, we generated mutations in individual or combinations of the WW domains. The rsp5-w1, rsp5-w2, and rsp5-w3 mutant alleles complement RSP5 deletions at 30 degrees. Thus, individual WW domains are not essential. Each rsp5-w mutation caused temperature-sensitive growth. Among variants with mutations in multiple WW domains, only rsp5-w1w2 complemented the deletion. Thus, the WW3 domain is sufficient for Rsp5p essential functions. To determine whether rsp5-w mutations affect endocytosis, fluid phase and uracil permease (Fur4p) endocytosis was examined. The WW3 domain is important for both processes. WW2 appears not to be important for fluid phase endocytosis whereas it is important for Fur4p endocytosis. In contrast, the WW1 domain affects fluid phase endocytosis, but it does not appear to function in Fur4p endocytosis. Thus, various WW domains play different roles in the endocytosis of these two substrates. Rsp5p is located in the cytoplasm in a punctate pattern that does not change during the cell cycle. Altering WW domains does not change the location of Rsp5p.
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