Abstract
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.
| Original language | English |
|---|---|
| Pages (from-to) | 21-32 |
| Number of pages | 12 |
| Journal | Progress in Cell Cycle Research |
| Volume | 1 |
| Publication status | Published - 1 Dec 1995 |
| Externally published | Yes |
Cite this
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Regulation of p70s6k/p85s6k and its role in the cell cycle. / Pearson, R. B.; Thomas, G.
In: Progress in Cell Cycle Research, Vol. 1, 01.12.1995, p. 21-32.Research output: Contribution to journal › Review Article › Research › peer-review
TY - JOUR
T1 - Regulation of p70s6k/p85s6k and its role in the cell cycle.
AU - Pearson, R. B.
AU - Thomas, G.
PY - 1995/12/1
Y1 - 1995/12/1
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0029418405&partnerID=8YFLogxK
M3 - Review Article
VL - 1
SP - 21
EP - 32
JO - Progress in Cell Cycle Research
JF - Progress in Cell Cycle Research
SN - 1087-2957
ER -