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(Received for publication, January 27, 1997, and in revised form, April 7, 1997)
From the Biochemistry Laboratory, School of Biological Sciences,
University of Sussex, Falmer, Brighton BN1 9QG, United Kingdom
The initiation factor (eIF) 4E is regulated by
modulating both the phosphorylation and the availability of the protein
to participate in the initiation process. Here we show that either serum treatment or activation of the stress-activated protein kinase
(JNK/SAPK) led to enhanced phosphorylation of eIF4E in quiescent NIH
3T3 cells. Although the immunosuppressant, rapamycin, was found to
stabilize the association of eIF4E with its negative regulator, 4E-BP1,
this drug did not prevent the early effects of serum stimulation on the
overall rate of translation, polysome formation, the phosphorylation
status of eIF4E, or the recruitment of eIF4E into the eIF4F complex.
However, the rapid enhancement of eIF4E phosphorylation in response to
serum was largely prevented by the inhibitor of mitogen-activated
protein (MAP) kinase activation, PD98059. Activation of the JNK/SAPK
signaling pathway with anisomycin resulted in enhanced phosphorylation
of eIF4E, which was prevented by either rapamycin or the highly
specific p38 MAP kinase inhibitor, SB203580. These data illustrate that
multiple signaling pathways, including those of distinct members of the
MAP kinase family, mediate the phosphorylation of eIF4E and that the
association of eIF4E with 4E-BP1 does not necessarily prevent
phosphorylation of eIF4E in vivo.
Volume 272, Number 28,
Issue of July 11, 1997
pp. 17887-17893
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
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