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Domains of the Rsp5 ubiquitin-protein ligase required for receptor-mediated and fluid-phase endocytosis.
| Content Provider | Semantic Scholar |
|---|---|
| Author | Dunn, Rebecca Hicke, Linda A. |
| Copyright Year | 2001 |
| 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. |
| File Format | PDF HTM / HTML |
| DOI | 10.1091/mbc.12.2.421 |
| PubMed reference number | 11179425 |
| Journal | Medline |
| Volume Number | 12 |
| Issue Number | 2 |
| Alternate Webpage(s) | http://www.molbiolcell.org/content/12/2/421.full.pdf |
| Alternate Webpage(s) | https://doi.org/10.1091/mbc.12.2.421 |
| Journal | Molecular biology of the cell |
| Language | English |
| Access Restriction | Open |
| Content Type | Text |
| Resource Type | Article |
