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J Biol Chem, Vol. 273, Issue 46, 30061-30064, November 13, 1998
Containing a Proline-rich Region
§,
,,,, and
From the A novel ribosomal S6 kinase, termed
p70 S6 kinase Ludwig Institute for Cancer Research,
London W1P 8BY and the Department of Biochemistry and Molecular
Biology, University College London, London WC1E 6BT, United Kingdom,
the § Institute of Molecular Biology and Genetics, Kyiv 143, Ukraine, and the Biosignal Research Center, Kobe University,
Kobe 657-8501, Japan
(p70), which has a highly conserved amino acid
sequence compared with that of p70/p85 S6 kinase (p70
) within the
catalytic, kinase extension, and autoinhibitory pseudosubstrate
domains, was identified. However, the amino acid sequence of p70
differs from that of p70 in the noncatalytic amino-terminal region
and in the carboxyl-terminal tail, which contains a proline-rich
region. The majority of the regulatory phosphorylation sites identified
in p70 are conserved in p70. Two isoforms of p70, referred to
as 1 (495 amino acids) and 2 (482 amino acids), could be
expressed from the single gene either by alternative mRNA splicing
or by the use of alternative start codons. Here we report the
characterization of p702. Similarly to p70, the catalytic
activity of p70 toward ribosomal protein S6 could be rapidly
activated by serum, insulin, and phorbol ester in transiently
transfected cells. The p70 kinase was found to be significantly less
sensitive to wortmannin and rapamycin than p70. These results
indicate that p70 has the potential to participate in the regulation
of protein synthesis and the cell cycle.
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