Regulation of actin dynamics by stress-activated protein kinase 2 (SAPK2)-dependent phosphorylation of heat-shock protein of 27 kDa (Hsp27)

Biochem Soc Symp. 1999;64:79-89.

Abstract

Activation of the mitogen-activated protein kinase (MAP kinase) SAPK2 (stress-activated protein kinase 2) leads to the phosphorylation of several transcription factors and cytoplasmic proteins, and thereby presumably orchestrates important specific cellular responses to numerous cytokines, stressing agents and agonists of tyrosine kinase or serpentine receptors. The heat-shock protein of 27 kDa (Hsp27), a downstream target of the SAPK2-activated MAP-kinase-activated protein kinase-2/3, has a documented function as an actin polymerization modulator. Accordingly, recent evidence implicates the SAPK2 pathway in the modulation of microfilament dynamics in response to stress and agonist stimulation. In vascular endothelial cells, where the basal level of expression of Hsp27 is high, SAPK2 mediates oxidative stress- and vascular endothelial growth factor (VEGF)-induced actin reorganization and VEGF-induced cell migration, suggesting a key role for this MAP kinase pathway in inflammation and angiogenic processes.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Actins / metabolism
  • Calcium-Calmodulin-Dependent Protein Kinases / metabolism*
  • Growth Substances / physiology
  • Heat-Shock Proteins / metabolism*
  • Humans
  • Mitogen-Activated Protein Kinases*
  • Oxidative Stress
  • Phosphorylation
  • p38 Mitogen-Activated Protein Kinases

Substances

  • Actins
  • Growth Substances
  • Heat-Shock Proteins
  • Calcium-Calmodulin-Dependent Protein Kinases
  • Mitogen-Activated Protein Kinases
  • p38 Mitogen-Activated Protein Kinases