BMK1 mediates growth factor-induced cell proliferation through direct cellular activation of serum and glucocorticoid-inducible kinase

J Biol Chem. 2001 Mar 23;276(12):8631-4. doi: 10.1074/jbc.C000838200. Epub 2001 Jan 31.

Abstract

Activation of the mammalian mitogen-activated protein kinase known as BMK1 is required for growth factor-induced cell proliferation. To understand the mechanism by which BMK1 mediates this cellular response, this kinase was used as bait in a yeast two-hybrid-based library screening. Here, we report the identification of serum and glucocorticoid-inducible kinase (SGK) as a cellular protein that physically interacts with BMK1. During growth factor-induced cell stimulation, BMK1 activates SGK by phosphorylation at serine 78. This BMK1-mediated phosphorylation event is necessary for the activation of SGK and, more importantly, for cell proliferation induced by growth factors.

Publication types

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

MeSH terms

  • Cell Division / physiology*
  • Enzyme Activation
  • Epidermal Growth Factor / physiology*
  • Immediate-Early Proteins
  • Mitogen-Activated Protein Kinase 7
  • Mitogen-Activated Protein Kinases / physiology*
  • Nuclear Proteins*
  • Phosphorylation
  • Protein Serine-Threonine Kinases / metabolism*

Substances

  • Immediate-Early Proteins
  • Nuclear Proteins
  • Epidermal Growth Factor
  • Protein Serine-Threonine Kinases
  • serum-glucocorticoid regulated kinase
  • Mitogen-Activated Protein Kinase 7
  • Mitogen-Activated Protein Kinases