Molecular and Biochemical Characterization of the Mitogen-Activated S6 Kinase

  • George Thomas
Conference paper
Part of the NATO ASI Series book series (volume 56)

Abstract

The approach generally taken to determine how growth factors induce cells to proliferate begins with purification of the growth factor and then using it to probe for its corresponding receptor. This has led to the finding that most growth factor receptors are tyrosine kinases and that binding of the growth factor to the receptor leads to an increase in this activity (for a review see Carpenter G, 1987; Yarden Y and Ulrich A, 1988). Results obtained from site-directed mutagenesis experiments further argue that the increase in this kinase activity is essential in conveying the mitogenic response (Carpenter G, 1987; Yarden Y and Ulrich A, 1988). Indeed, it is thought that the mitogenic response is propagated through a cascade of kinase reactions which are initiated by the tyrosine kinase receptor (Czech MP et al, 1988; Carpenter G and Cohen S, 1990). In our laboratory we have approached this question from inside the cell. We have begun with an obligatory step in the mitogenic response, the activation of protein synthesis, shown how this event may be triggered by the multiple phosphorylation of a ribosomal protein, S6, and attempted to trace the pathway back to the cell membrane describing the molecular components which are involved in the activation of this process (Kozma SC et al, 1989a; Hershey JWB, 1989).

Keywords

Tyrosine Vanadate Serine Polypeptide Phenylalanine 

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References

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Copyright information

© Springer-Verlag Berlin Heidelberg 1991

Authors and Affiliations

  • George Thomas
    • 1
  1. 1.Friedrich Miescher InstituteBaselSwitzerland

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