Loss of Rb overrides the requirement for ERK activity for cell proliferation

J Cell Sci. 2002 Dec 1;115(Pt 23):4607-16. doi: 10.1242/jcs.00161.

Abstract

The Ras GTPase is a critical transducer of mitogenic signals ultimately leading to inactivation of the retinoblastoma (Rb) protein, but the molecular basis underlying Ras-dependent control of cell cycle kinetics remains to a great extent unknown. In an effort to further elucidate the role of Ras activation in cell cycle control, we have studied the role of the downstream Mek-ERK pathway in facilitating exit from the quiescent G0 state and passage through the G1/S transition. We have adopted a genetic approach in combination with U0126, an inhibitor of Mek activation to study the role of Mek in cell cycle progression. Here we report that whereas wild-type (Wt) mouse embryo fibroblasts (MEFs) depend on ERK activation to enter the cell cycle, Rb-deficient (Rb(-/-)) MEFs have a reduced requirement for ERK signalling. Indeed in the presence of U0126 we found that Rb-null MEFs can exit G0, make the G1/S transition and proliferate. Analysis of Rb-deficient tumour cell lines also revealed a reduced requirement for ERK signalling in asynchronous growth. We discuss the molecular mechanism that may underlie this escape from MAP kinase signalling.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Butadienes / pharmacology
  • Cell Division / drug effects
  • Cells, Cultured
  • Chromones / pharmacology
  • Cyclin-Dependent Kinase 4
  • Cyclin-Dependent Kinases / metabolism
  • Cyclins / metabolism
  • Gene Deletion
  • Gene Expression Regulation / drug effects
  • MAP Kinase Signaling System / drug effects
  • Mice
  • Mitogen-Activated Protein Kinase Kinases / antagonists & inhibitors
  • Mitogen-Activated Protein Kinase Kinases / metabolism
  • Mitogen-Activated Protein Kinases / metabolism*
  • Morpholines / pharmacology
  • Nitriles / pharmacology
  • Phosphatidylinositol 3-Kinases / metabolism
  • Phosphorylation / drug effects
  • Proto-Oncogene Proteins*
  • Retinoblastoma Protein / genetics
  • Retinoblastoma Protein / metabolism*
  • Time Factors
  • Tumor Cells, Cultured

Substances

  • Butadienes
  • Chromones
  • Cyclins
  • Morpholines
  • Nitriles
  • Proto-Oncogene Proteins
  • Retinoblastoma Protein
  • U 0126
  • 2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one
  • Phosphatidylinositol 3-Kinases
  • Cdk4 protein, mouse
  • Cyclin-Dependent Kinase 4
  • Cyclin-Dependent Kinases
  • Mitogen-Activated Protein Kinases
  • Mitogen-Activated Protein Kinase Kinases