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Related Experiment Videos

Multiple pathways for activation of MAP kinases

G Mitra1, M Weber, D Stacey

  • 1Department of Molecular Biology, Cleveland Clinic Foundation, OH.

Cellular & Molecular Biology Research
|January 1, 1993
PubMed
Summary
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Mitogen-activated protein kinase (MAPK) and MAP Kinase Kinase (MAPKK) are elevated in v-raf transformed cells. Both c-ras dependent and independent pathways contribute to MAPK activation, beyond the known c-Raf-1 kinase.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Signal Transduction

Background:

  • Mitogen-activated protein kinase (MAPK) and MAP Kinase Kinase (MAPKK) activities are elevated in v-raf transformed NIH3T3 cells.
  • This elevation correlates with increased tyrosine phosphorylation of p42mapk protein.
  • Further enhancement of these activities can be achieved with serum, tetradecanoyl phorbol acetate (TPA), or aluminium fluoride.

Purpose of the Study:

  • To investigate the pathways involved in MAPK activation in v-raf transformed cells.
  • To determine the role of c-ras dependent and independent pathways in MAPK activation.
  • To compare MAPK activation in cells expressing v-raf alone versus coexpressing v-raf and a dominant inhibitory ras mutant.

Main Methods:

  • Utilized NIH3T3 cell lines, including v-raf transformed cells and a cell line (M17raf) coexpressing v-raf and N-17 ras.

Related Experiment Videos

  • Measured MAPK and MAPKK activities.
  • Assessed tyrosine phosphorylation of p42mapk protein.
  • Treated cells with serum, TPA, and aluminium fluoride to evaluate pathway responses.

    • Main Results:

    • Constitutively elevated MAPK and MAPKK activities were observed in v-raf transformed cells.
    • Serum, TPA, and aluminium fluoride moderately enhanced MAPK activity in raf-transformed cells.
    • In M17raf cells, serum and TPA-stimulated MAPK activity was reduced, while aluminium fluoride remained potent.
    • Similar MAPK activation was observed in M17raf cells compared to similarly treated raf-transformed cells.

    Conclusions:

    • c-Raf-1, a serine/threonine kinase, is an upstream activator of MAPK.
    • Both c-ras dependent and c-ras independent pathways contribute to MAPK activation.
    • These findings elucidate complex signaling networks regulating MAPK activation in cellular transformation.