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Interaction of the CDK2-associated protein-1, p12(DOC-1/CDK2AP1), with its homolog, p14(DOC-1R)

Waranun Buajeeb1, Xue Zhang, Hiroe Ohyama

  • 1Department of Oral Medicine, Faculty of Dentistry, Mahidol University, Bangkok, Thailand.

Biochemical and Biophysical Research Communications
|February 27, 2004
PubMed

Insights

The human DOC-1/CDK2AP1 protein interacts with its homolog, p14(DOC-1R). This discovery clarifies the role of p12(DOC-1/CDK2AP1) in cell cycle regulation and carcinogenesis.

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Genetics

Background:

  • The human DOC-1/CDK2AP1 gene encodes a 12kDa growth suppressor protein, p12(DOC-1/CDK2AP1).
  • p12(DOC-1/CDK2AP1) interacts with cell cycle proteins like CDK2 and DNA polymerase alpha/primase, suppressing DNA replication and regulating CDK2 activity.
  • Understanding p12(DOC-1/CDK2AP1) interactions is crucial for elucidating its role in cell cycle control and cancer development.

Purpose of the Study:

  • To identify novel interacting proteins of p12(DOC-1/CDK2AP1) using a yeast two-hybrid system.
  • To further investigate the functional implications of p12(DOC-1/CDK2AP1) in cellular processes.

Main Methods:

  • Yeast two-hybrid screening using human p12(DOC-1/CDK2AP1) as bait against a human liver cDNA library.
  • In vitro and cellular interaction validation using GST pull-down assays and immunoprecipitation.
  • Deletion mutant analysis to map the interaction domain between p12(DOC-1/CDK2AP1) and p14(DOC-1R).

Main Results:

  • Identification of cDNA clones encoding human DOC-1R transcript interacting with p12(DOC-1/CDK2AP1).
  • Confirmation of the physical interaction between p12(DOC-1/CDK2AP1) and p14(DOC-1R) in vitro and within cells.
  • Localization of the critical interaction region to amino acids 20-25 of p12(DOC-1/CDK2AP1).

Conclusions:

  • p12(DOC-1/CDK2AP1) physically associates with its homologous protein, p14(DOC-1R).
  • This interaction provides new insights into the molecular mechanisms governing cell cycle regulation and potentially carcinogenesis.

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