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(Received for publication, May 9, 1996, and in revised form, September 11, 1996)
From the The eukaryotic initiation factor 4E
(eIF-4E)-binding proteins PHAS-I and PHAS-II were found to have
overlapping but different patterns of expression in tissues. Both PHAS
proteins were expressed in 3T3-L1 adipocytes, in which insulin
stimulated their phosphorylation, promoted dissociation of
PHAS·eIF-4E complexes, and decreased the ability of both to bind
exogenous eIF-4E. The effects of insulin were attenuated by rapamycin
and wortmannin, two agents that block activation of p70S6K.
Unlike PHAS-I, PHAS-II was readily phosphorylated by
cAMP-dependent protein kinase in vitro;
however, the effects of insulin on both PHAS proteins were attenuated
by agents that increase intracellular cAMP, by cAMP derivatives, and by
phosphodiesterase inhibitors. These agents also markedly inhibited the
activation of p70S6K. In summary, our results indicate that
PHAS-I and -II are controlled by the mammalian target of rapamycin and
p70S6K signaling pathway and that in 3T3-L1 adipocytes this
pathway is inhibited by increased cAMP.
Volume 271, Number 47,
Issue of November 22, 1996
pp. 30199-30204
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
and§
Department of Molecular Biology and
Pharmacology, Washington University School of Medicine, St. Louis,
Missouri 63110 and § Departments of Pharmacology and
Medicine, University of Virginia School of Medicine,
Charlottesville, Virginia 22908
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