Negative regulation of MEKK1-induced signaling by glutathione S-transferase Mu

J Biol Chem. 2004 Oct 15;279(42):43589-94. doi: 10.1074/jbc.M404359200. Epub 2004 Aug 6.

Abstract

Mitogen-activated protein kinase/extracellular signal-regulated kinase kinase kinase 1 (MEKK1) is an important component in the stress-activated protein kinase pathway. Glutathione S-transferase Mu 1-1 (GST M1-1) has now been shown to inhibit the stimulation of MEKK1 activity induced by cellular stresses such as UV and hydrogen peroxide. GST M1-1 inhibited MEKK1 activation in a manner independent of its glutathione-conjugating catalytic activity. In vitro binding and kinase assays revealed that GST M1-1 directly bound MEKK1 and inhibited its kinase activity. Co-immunoprecipitation analysis showed a physical association between endogenous GST M1-1 and endogenous MEKK1 in L929 cells. Overexpressed GST M1-1 interfered with the binding of MEKK1 to SEK1 in transfected HEK293 cells. Furthermore, GST M1-1 suppressed MEKK1-mediated apoptosis. Taken together, our results suggest that GST M1-1 functions as a negative regulator of MEKK1.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cell Line
  • Cloning, Molecular
  • Glutathione Transferase / metabolism*
  • Humans
  • Kinetics
  • L Cells
  • MAP Kinase Kinase Kinase 1 / antagonists & inhibitors
  • MAP Kinase Kinase Kinase 1 / metabolism*
  • Mice
  • Recombinant Proteins / metabolism
  • Signal Transduction / physiology*

Substances

  • Recombinant Proteins
  • Glutathione Transferase
  • MAP Kinase Kinase Kinase 1