Kinase suppressor of ras is necessary for tumor necrosis factor alpha activation of extracellular signal-regulated kinase/mitogen-activated protein kinase in intestinal epithelial cells

Cancer Res. 2001 Feb 1;61(3):963-9.

Abstract

Mitogen-activated protein (MAP) kinase activity is essential for tumor necrosis factor (TNF) alpha receptor 1 regulation of intestinal epithelial cell proliferation. However, the mechanism of TNF-alpha mediated activation of extracellular signal-regulated kinase (ERK)/M1AP kinase has not been established clearly. Both TNF-alpha and cell-permeable ceramide have been reported to increase the kinase activity of kinase suppressor of Ras (KSR). To determine the role of KSR in TNF-alpha-induced ERK1/ERK2 activation, we studied young adult mouse colon cells expressing a dominant-negative, kinase-inactive (ki) KSR. We report that TNF-alpha, a cell-permeable ceramide, and sphingomyelinase stimulate ERK1/ERK2 activation and increase the phosphoserine content of KSR, which are inhibited by kiKSR expression in intact cells. Furthermore, TNF-alpha-induced Raf-1 threonine phosphorylation, kinase activity toward MEK1, and association with KSR are also inhibited by kiKSR expression. Our data also show by sequential in vitro kinase assays that TNF-alpha enhances KSR phosphorylation of Raf-1 on threonine, enhancing Raf-1 kinase activity toward MAP kinase kinase. We therefore conclude that KSR is an essential upstream regulator of TNF-alpha-stimulated ERK1/ERK2 activation, most likely mediated via direct phosphorylation of Raf-1.

Publication types

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

MeSH terms

  • Animals
  • Cell Line
  • Ceramides / pharmacology
  • Colon / cytology
  • Colon / enzymology*
  • Enzyme Activation
  • Epithelial Cells / enzymology
  • Intestinal Mucosa / enzymology*
  • JNK Mitogen-Activated Protein Kinases*
  • MAP Kinase Kinase 1
  • MAP Kinase Kinase 4
  • MAP Kinase Signaling System / drug effects
  • Mice
  • Mitogen-Activated Protein Kinase 1 / metabolism*
  • Mitogen-Activated Protein Kinase 3
  • Mitogen-Activated Protein Kinase Kinases / metabolism
  • Mitogen-Activated Protein Kinases / metabolism*
  • Phosphorylation
  • Phosphoserine / metabolism
  • Phosphothreonine / metabolism
  • Protein Kinases / metabolism
  • Protein Kinases / physiology*
  • Protein Serine-Threonine Kinases / metabolism
  • Proto-Oncogene Proteins c-raf / metabolism
  • Sphingomyelin Phosphodiesterase / pharmacology
  • Tumor Necrosis Factor-alpha / antagonists & inhibitors
  • Tumor Necrosis Factor-alpha / pharmacology*
  • Tumor Necrosis Factor-alpha / physiology

Substances

  • Ceramides
  • Tumor Necrosis Factor-alpha
  • Phosphothreonine
  • Phosphoserine
  • Protein Kinases
  • KSR-1 protein kinase
  • Protein Serine-Threonine Kinases
  • Proto-Oncogene Proteins c-raf
  • JNK Mitogen-Activated Protein Kinases
  • Mitogen-Activated Protein Kinase 1
  • Mitogen-Activated Protein Kinase 3
  • Mitogen-Activated Protein Kinases
  • MAP Kinase Kinase 1
  • MAP Kinase Kinase 4
  • Map2k1 protein, mouse
  • Mitogen-Activated Protein Kinase Kinases
  • Sphingomyelin Phosphodiesterase