ArticleMolecular biology of the cell2001
Domains of the Rsp5 ubiquitin-protein ligase required for receptor-mediated and fluid-phase endocytosis.
Article in Molecular biology of the cell, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.
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Who cites it
62 citing papers in PubMed, 137 citations in OpenAlex.
- Septin organization is regulated by the Gpa1 ubiquitination domain and endocytic machinery during the yeast pheromone response.Molecular biology of the cell · 2025Article
- Unremodeled GPI-anchored proteins at the plasma membrane trigger aberrant endocytosis.Life science alliance · 2025Article
- USP34 regulates endothelial PAR1 mRNA transcript expression and cellular signaling.Molecular biology of the cell · 2025Article
- Nicotinamide Antagonizes Lipopolysaccharide-Induced Hypoxic Cell Signals in Human Macrophages.Journal of immunology (Baltimore, Md. : 1950) · 2023Article
- A novel yeast-based screening system for potential compounds that can alleviate human α-synuclein toxicity.Journal of applied microbiology · 2022Article
- Regulation of the endocytosis and prion-chaperoning machineries by yeast E3 ubiquitin ligase Rsp5 as revealed by orthogonal ubiquitin transfer.Cell chemical biology · 2021Article
- Adaptors as the regulators of HECT ubiquitin ligases.Cell death and differentiation · 2021Review
- Endocytosis of nutrient transporters in fungi: The ART of connecting signaling and trafficking.Computational and structural biotechnology journal · 2021Review
- GPCR receptor phosphorylation and endocytosis are not necessary to switch polarized growth between internal cues during pheromone response inCommunicative & integrative biology · 2020Article
- 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
- Sodium Acetate Responses inFrontiers in microbiology · 2018Review
- The exocyst subunit Sec3 is regulated by a protein quality control pathway.The Journal of biological chemistry · 2017Article
- Self-regulating ubiquitin ligases.The EMBO journal · 2017Article
- Ubiquitylation-dependent oligomerization regulates activity of Nedd4 ligases.The EMBO journal · 2017Article
- Article
- Clathrin-mediated endocytosis in budding yeast at a glance.Journal of cell science · 2016Review
- Loss of vacuolar H+-ATPase activity in organelles signals ubiquitination and endocytosis of the yeast plasma membrane proton pump Pma1p.The Journal of biological chemistry · 2014Article
- Review
- Specific α-arrestins negatively regulate Saccharomyces cerevisiae pheromone response by down-modulating the G-protein-coupled receptor Ste2.Molecular and cellular biology · 2014Article
2 more citing papers are in PubMed but not listed here.
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2 authors at 1 institution in 1 country.
Funding
Abstract
Yeast Rsp5p and its mammalian homologue, Nedd4, are hect domain ubiquitin-protein ligases (E3s) required for the ubiquitin-dependent endocytosis of plasma membrane proteins. Because ubiquitination is sufficient to induce internalization, E3-mediated ubiquitination is a key regulatory event in plasma membrane protein endocytosis. Rsp5p is an essential, multidomain protein containing an amino-terminal C2 domain, three WW protein-protein interaction domains, and a carboxy-terminal hect domain that carries E3 activity. In this study, we demonstrate that Rsp5p is peripherally associated with membranes and provide evidence that Rsp5p functions as part of a multimeric protein complex. We define the function of Rsp5p and its domains in the ubiquitin-dependent internalization of the yeast alpha-factor receptor, Ste2p. Temperature-sensitive rsp5 mutants were unable to ubiquitinate or to internalize Ste2p at the nonpermissive temperature. Deletion of the entire C2 domain had no effect on alpha-factor internalization; however, point mutations in any of the three WW domains impaired both receptor ubiquitination and internalization. These observations indicate that the WW domains play a role in the important regulatory event of selecting phosphorylated proteins as endocytic cargo. In addition, mutations in the C2 and WW1 domains had more severe defects on transport of fluid-phase markers to the vacuole than on receptor internalization, suggesting that Rsp5p functions at multiple steps in the endocytic pathway.
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