Activation of the MAP kinase homologue RK requires the phosphorylation of Thr-180 and Tyr-182 and both residues are phosphorylated in chemically stressed KB cells

FEBS Lett. 1995 May 8;364(2):223-8. doi: 10.1016/0014-5793(95)00346-b.

Abstract

A MAP kinase homologue, termed the reactivating kinase (RK), lies in a signalling pathway which mediates cellular responses to stress. Here we demonstrate that the stress-induced activation of the RK in human KB cells is accompanied by the phosphorylation of Thr-180 and Tyr-182, and that the phosphorylation of both residues is required for the activation of this enzyme.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • Cell Line
  • DNA, Complementary / genetics
  • Enzyme Activation
  • Humans
  • Intracellular Signaling Peptides and Proteins
  • Molecular Sequence Data
  • Mutation
  • Peptide Fragments / chemistry
  • Peptide Fragments / genetics
  • Phosphorylation
  • Protein Kinases*
  • Protein-Serine-Threonine Kinases / chemistry
  • Protein-Serine-Threonine Kinases / genetics
  • Protein-Serine-Threonine Kinases / metabolism*
  • Protein-Tyrosine Kinases / chemistry
  • Protein-Tyrosine Kinases / genetics
  • Protein-Tyrosine Kinases / metabolism*
  • Xenopus
  • Xenopus Proteins*

Substances

  • DNA, Complementary
  • Intracellular Signaling Peptides and Proteins
  • Peptide Fragments
  • Xenopus Proteins
  • Protein Kinases
  • MAP-kinase-activated kinase 2
  • Mpk2 protein, Xenopus
  • Protein-Tyrosine Kinases
  • Protein-Serine-Threonine Kinases