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(Received for publication, July 13, 1995; and in revised form, October 23, 1995)
We show here using synchronized Swiss mouse 3T3 fibroblasts that
p70 S6 kinase (p70) and mitogen-activated
protein kinases
(p42
/p44
) are not only
activated at the G
/G
boundary, but also in
cells progressing from M into G. p70 activity increases 20-fold in G
cells released
from G. Throughout G, S, and G
it
decreases constantly, so that during M phase low kinase activity is
measured. The kinase is reactivated 10-fold when cells released from a
nocodazole-induced metaphase block enter G of the next cell
cycle. p42/p44
in
G
cells are activated transiently early in G and are reactivated late in mitosis after nocodazole release.
p70activity is dependent on permanent signaling
from growth factors at all stages of the cell cycle. Immunofluorescence
studies showed that p70
and its isoform
p85
become concentrated in localized spots in
the nucleus at certain stages in the cell cycle. Cell cycle-dependent
changes in p70
activity are associated with
alterations in the phosphorylation state of the protein. However,
examination of the regulation of a p70
mutant in
which the four carboxyl-terminal phosphorylation sites are changed to
acidic amino acids suggests that a mechanism independent of these
phosphorylation sites controls the activity of the enzyme during the
cell cycle.
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