• Medicine
  • Published in
    The Journal of biological…
    2000

Dephosphorylation of human cyclin-dependent kinases by protein phosphatase type 2C alpha and beta 2 isoforms.

@article{Cheng2000DephosphorylationOH,
  title={Dephosphorylation of human cyclin-dependent kinases by protein phosphatase type 2C alpha and beta 2 isoforms.},
  author={Aiyang Cheng and Philipp Kaldis and Michael J. Solomon},
  journal={The Journal of biological chemistry},
  year={2000},
  volume={275 44},
  pages={
          34744-9
        }
}
We previously reported that the activating phosphorylation on cyclin-dependent kinases in yeast (Cdc28p) and in humans (Cdk2) is removed by type 2C protein phosphatases. In this study, we characterize this PP2C-like activity in HeLa cell extract and determine that it is due to PP2C beta 2, a novel PP2C beta isoform, and to PP2C alpha. PP2C alpha and PP2C beta 2 co-purified with Mg(2+)-dependent Cdk2/Cdk6 phosphatase activity in DEAE-Sepharose, Superdex-200, and Mono Q chromatographies. Moreover… CONTINUE READING

Citations

Publications citing this paper.
SHOWING 1-10 OF 42 CITATIONS

The Human Polo-like Kinase 4 is a Regulator of Centrosome Duplication

VIEW 27 EXCERPTS
CITES BACKGROUND
HIGHLY INFLUENCED

Activation of Protein Serine/Threonine Phosphatase PP2Cα Efficiently Prevents Liver Fibrosis

VIEW 3 EXCERPTS
CITES BACKGROUND
HIGHLY INFLUENCED

Role of PP2Cα in cell growth, in radio- and chemosensitivity, and in tumorigenicity

VIEW 9 EXCERPTS
CITES BACKGROUND & RESULTS
HIGHLY INFLUENCED

Biochemical characterization of Cdk2-Speedy/Ringo A2

VIEW 7 EXCERPTS
CITES METHODS & BACKGROUND