| Message: | A Cdk-interacting protein called Cdi1 (cyclin-dependent kinase interactor 1)/KAP (kinase associated phosphatase) was first identified as a novel G1- and S-phase dual-specificity phosphatase that associates with Cdk2 and/or Cdc2 by the interaction trap, a yeast genetic selection for interacting proteins. Using yeast two hybrid system, Cdi1/KAP interacts with cyclin-dependent kinases, including human Cdc2, Cdk2 and Cdk3, but not with Cdk4. In HeLa cells, Cdi1/KAP is expressed at the G1 to S transition, and the protein forms stable complexes with Cdk2. Further studies demonstrated that Cdi1/KAP binds to Cdk2 and dephosphorylates Thr160 when the associated cyclin subunit is degraded or dissociated. It means that Cdi1/KAP may inactivate a Cdk2 or Cdc2, by removing phosphates from the cyclin complexes, and this may contribute to cell cycle control. However, the physiological substrate(s) for tyrosine dephosphorylation of Cdi1/KAP has not yet been identified.
https://www.creativebiomart.net/protein-phosphatase-cdi1kap-fluorometric-human-assay-kit-463633.htm |
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