Negative influence of RasG on chemoattractant-induced ERK2 phosphorylation in Dictyostelium

Biochim Biophys Acta. 1998 Mar 12;1402(1):1-5. doi: 10.1016/s0167-4889(98)00010-x.

Abstract

The Dictyostelium ERK2 protein is transiently activated when cells are treated with the chemotactic agents cAMP or folic acid. Activating phosphorylation is markedly inhibited in strains overexpressing the constitutively activated RasG protein. This is in marked contrast to mammalian cells where the highly related mitogen-activated protein kinases (MAPKs) are stimulated by Ras activation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Calcium-Calmodulin-Dependent Protein Kinases / metabolism*
  • Chemotactic Factors / pharmacology*
  • Cyclic AMP / pharmacology*
  • Dictyostelium / drug effects
  • Dictyostelium / metabolism*
  • Folic Acid / pharmacology*
  • Kinetics
  • Mitogen-Activated Protein Kinase 1
  • Phosphorylation
  • Phosphotyrosine / metabolism
  • Point Mutation
  • RNA, Messenger / biosynthesis
  • Recombinant Proteins / metabolism
  • Signal Transduction
  • Transcription, Genetic

Substances

  • Chemotactic Factors
  • RNA, Messenger
  • Recombinant Proteins
  • Phosphotyrosine
  • Folic Acid
  • Cyclic AMP
  • Calcium-Calmodulin-Dependent Protein Kinases
  • Mitogen-Activated Protein Kinase 1