The adenovirus E1A-associated kinase consists of cyclin E-p33cdk2 and cyclin A-p33cdk2

J Virol. 1993 May;67(5):2456-65. doi: 10.1128/JVI.67.5.2456-2465.1993.

Abstract

The adenovirus E1A oncoproteins form stable complexes with several cellular proteins. Association of E1A with these proteins has been shown to be important for the oncogenic potential of E1A. Several of these proteins have been identified and include the product of the retinoblastoma gene and a key cell cycle regulatory protein, cyclin A. E1A also associates with a potent histone H1 kinase. The two major components of this activity are the cyclin E-p33cdk2 and cyclin A-p33cdk2 complexes. Both the cyclin E-p33cdk2 and cyclin A-p33cdk2 complexes have been implicated in regulatory events controlling entry into or passage through DNA synthesis. Although the architecture of such interactions remains unclear, it is likely that by targeting such complexes, adenovirus is affecting some aspect of cell cycle control.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Adenovirus E1A Proteins / metabolism*
  • Adenoviruses, Human / enzymology*
  • Cell Cycle / physiology
  • Cells, Cultured
  • Cyclins / metabolism*
  • Humans
  • Protamine Kinase / metabolism*
  • Protein Serine-Threonine Kinases / metabolism*

Substances

  • Adenovirus E1A Proteins
  • Cyclins
  • Protamine Kinase
  • Protein Serine-Threonine Kinases