Abstract
In numerous biological systems activation of cell growth is closely coupled to the multiple phosphorylation of 40S ri-bosomal protein S6. This event appears to be a prerequisite for an associated increase in the overall rate of protein synthesis and to a number of specific alterations in the pattern of translation.1–4 The purpose of this lecture is three fold. First, to present the background and rationale for studying S6 phosphorylation during the mitogenic response. Second, to review a number of key experiments concerning the possible role of this event in the control of protein synthesis and how it may be regulated. Finally, to outline the types of questions which are now being asked and in what direction the field must advance in the near future.
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© 1987 Plenum Press, New York
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Thomas, G. (1987). Growth Factor-Mediated Activation of S6 Phosphorylation and Protein Synthesis. In: Heilmeyer, L.M.G. (eds) Signal Transduction and Protein Phosphorylation. NATO ASI Series, vol 135. Springer, Boston, MA. https://doi.org/10.1007/978-1-4757-0166-1_50
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DOI: https://doi.org/10.1007/978-1-4757-0166-1_50
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