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p12(DOC-1) is a novel cyclin-dependent kinase 2-associated protein

  1. Author:
    Shintani, S.
    Ohyama, H.
    Zhang, X.
    McBride, J.
    Matsuo, K.
    Tsuji, T.
    Hu, M. G.
    Hu, G. F.
    Kohno, Y.
    Lerman, M.
    Todd, R.
    Wong, D. T. W.

  2. Author Address

    Wong DTW Harvard Univ, Sch Dent Med, Lab Mol Pathol 188 Longwood Ave Boston, MA 02115 USA Harvard Univ, Sch Dent Med, Lab Mol Pathol Boston, MA 02115 USA Harvard Univ, Sch Dent Med, Lab Oral & Maxillofacial Surg Boston, MA 02115 USA Harvard Univ, Sch Med, Ctr Biochem & Biophys Sci & Med Boston, MA 02115 USA China Med Univ, Dept Cell Biol Shenyang Peoples R China NCI, Frederick Canc Res & Dev Ctr, SAIC Fredrick, Intramural Res Support Program Ft Detrick, MD 21702 USA NCI, Frederick Canc Res & Dev Ctr, DBS, Immunobiol Lab Ft Detrick, MD 21702 USA
    1. Year: 2000
  2. Journal: Molecular and Cellular Biology
    1. 20
    2. 17
    3. Pages: 6300-6307
  4. Type of Article: Article
  1. Abstract:

    Regulated cyclin-dependent kinase (CDK) levels and activities are critical for the proper progression of the cell division cycle, p12(DOC-1) is a growth suppressor isolated from normal keratinocytes. We report that p(12DOC-1) associates with CDK2. More specifically, p12(DOC-1) associates with the monomeric nonphosphorylated form of CDK2 (p33CDK2). Ectopic expression of p12(DOC-1) resulted in decreased cellular CDK2 and reduced CDK2-associated kinase activities and was accompanied by a shift in the cell cycle positions of p12(DOC-1) transfectants ( up arrow G(I) and down arrow S), The p12(DOC-1)-mediated decrease of CDK2 was prevented if the p12(DOC-1\) transfectants were grown in the presence of the proteosome inhibitor clasto-lactacystin beta-lactone, suggesting that p12(DOC-1) may target CDK2 for proteolysis. A CDK2 binding mutant was created and was found to revert p12(DOC-1)-mediated, CDK2-associated cell cycle phenotypes. These data support p12(DOC-1) as a specific CDK2-associated protein that negatively regulates CDK2 activities by sequestering the monomeric pool of CDK2, and/or targets CDK2 for proteolysis, reducing the active pool of CDK2. [References: 15]

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