Two to three-fold increases in the rate of protein synthesis are required both to enter the G1 phase of the cell cycle from G0 and to proceed to S phase in response to growth factors and mitogens. This increase is in part regulated via multiple phosphorylation of the 40S ribosomal protein S6 by the mitogen-stimulated p70s6k/p85s6k. At the protein synthesis level this event appears to be involved in specifically increasing the efficiency of translation of a family of essential mRNAs containing a polypyrimidine tract at their 5' transcriptional start site. The activation of p70s6k/p85s6k and maintenance of its activity throughout G1 is controlled via multiple phosphorylation events mediated by a complex signalling network acting on distinct sets of phosphorylation sites.
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