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Cdil , a Human G l and S Phase Protein Phosphatase That Associates w ith Cdk 2
| Content Provider | Semantic Scholar |
|---|---|
| Author | Gyuris, ’. Érica Golemis Helen Chettkov Roger Brent |
| Abstract | We used the interaction trap, a yeast genetic selection for interacting proteins, to isolate human cyclindependent kinase interactor 1 (Cdil). In yeast, Cdil interacts with cyclin-dependent kinases, including human CdcP, Cdk2, and Cdk3, but not with Ckd4. In HeLa cells, Cdil is expressed at the Gl to S transition, and the protein forms stable complexes with Cdk2. Cdil bears weak sequence similarity to known tyrosine and dual specificity phosphatases. In vitro, Cdil removes phosphate from tyrosine residues in model substrates, but a mutant protein that bears a lesion in the putative active site cysteine does not. Overexpression of wildtype Cdil delays progression through the cell cycle in yeast and HeLa cells; delay is dependent on Cdil phosphatase activity. These experiments identify Cdil as a novel type of protein phosphatase that forms complexes with cyclin-dependent kinases. |
| File Format | PDF HTM / HTML |
| Alternate Webpage(s) | http://brentlab.fredhutch.org/content/dam/stripe/brent/files/17.pdf |
| Language | English |
| Access Restriction | Open |
| Content Type | Text |
| Resource Type | Article |
