Np95 is regulated by E1A during mitotic reactivation of terminally differentiated cells and is essential for S phase entry

J Cell Biol. 2002 Jun 10;157(6):909-14. doi: 10.1083/jcb.200201025. Epub 2002 Jun 10.

Abstract

Terminal differentiation exerts a remarkably tight control on cell proliferation. However, the oncogenic products of DNA tumor viruses, such as adenovirus E1A, can force postmitotic cells to proliferate, thus representing a powerful tool to study progression into S phase. In this study, we identified the gene encoding Np95, a murine nuclear phosphoprotein, as an early target of E1A-induced transcriptional events. In terminally differentiated (TD) cells, the activation of Np95 was specifically induced by E1A, but not by overexpression of E2F-1 or of the cyclin E (cycE)-cyclin-dependent kinase 2 (cdk2) complex. In addition, the concomitant expression of Np95 and of cycE-cdk2 was alone sufficient to induce S phase in TD cells. In NIH-3T3 cells, the expression of Np95 was tightly regulated during the cell cycle, and its functional ablation resulted in abrogation of DNA synthesis. Thus, expression of Np95 is essential for S phase entry. Previous evidence suggested that E1A, in addition to its well characterized effects on the pRb/E2F-1 pathway, activates a parallel and complementary pathway that is also required for the reentry in S phase of TD cells (Tiainen, M., D. Spitkousky, P. Jansen-Dürr, A. Sacchi, and M. Crescenzi. 1996. Mol. Cell. Biol. 16:5302-5312). From our results, Np95 appears to possess all the characteristics to represent the first molecular determinant identified in this pathway.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • 3T3 Cells
  • Adenovirus E1A Proteins / physiology*
  • Animals
  • CCAAT-Enhancer-Binding Proteins
  • CDC2-CDC28 Kinases*
  • Cell Cycle
  • Cell Differentiation
  • Cell Division
  • Cell Line
  • Cell Nucleus / chemistry
  • Cyclin E / metabolism
  • Cyclin-Dependent Kinase 2
  • Cyclin-Dependent Kinases / metabolism
  • DNA, Viral / physiology
  • Enzyme Activation
  • Gene Expression Regulation
  • Kinetics
  • Mice
  • Muscle, Skeletal / cytology
  • Nuclear Proteins / chemistry
  • Nuclear Proteins / physiology*
  • Phosphoproteins / chemistry
  • Protein Serine-Threonine Kinases / metabolism
  • S Phase / physiology*
  • Ubiquitin-Protein Ligases

Substances

  • Adenovirus E1A Proteins
  • CCAAT-Enhancer-Binding Proteins
  • Cyclin E
  • DNA, Viral
  • Nuclear Proteins
  • Phosphoproteins
  • Ubiquitin-Protein Ligases
  • Uhrf1 protein, mouse
  • Protein Serine-Threonine Kinases
  • CDC2-CDC28 Kinases
  • Cdk2 protein, mouse
  • Cyclin-Dependent Kinase 2
  • Cyclin-Dependent Kinases