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(Received for publication, March 14, 1996, and in revised form, September 6, 1996)
From the Each of the three known mammalian
90-kDa S6 kinase (pp90rsk) isoforms (RSK1, RSK2, and RSK3) was
expressed in transfected cells and further characterized. The kinase
activity (immunocomplex toward S6 peptide) of each isoform was
activated by in vivo growth factor (epidermal growth factor
(EGF)) stimulation; RSK1 was more responsive (10-15-fold)
versus RSK2 and RSK3 (2-4-fold). Pretreatment with PD98059
(MEK1 inhibitor) partially (80%) blocked EGF-mediated ERK1 activation
and had similar effects on EGF stimulation of each ribosomal S6 kinase
(RSK). Cotransfection with dominant-negative MEK1 inhibited activation
of each RSK; furthermore, the kinase activity of RSK1, RSK2, and RSK3
was markedly increased by cotransfection with constitutively active
MEK1. A specific association between mitogen-activated protein kinases
(MAPKs) (ERK1 and ERK2) and RSK isoforms was tested by MAPK
immunoblotting after immunoprecipitation of RSKs. ERK1 and ERK2 were
present in RSK3 (and to a lesser extent, RSK2) immunoprecipitates, but
were absent in RSK1 immunoprecipitates. Both dephosphorylated (from
quiescent cells) and phosphorylated (from stimulated cells) MAPKs were
associated with RSK2 and RSK3. Deletion mutants of RSK3 were
characterized: the C terminus (33 residues) was shown to be required
for association with MAPKs. The kinase activity of RSK1 or RSK2 was
enhanced by in vitro incubation with ERK1. In contrast,
RSK3 activity was not affected by exposure to ERK1. Furthermore, MAPKs
in RSK3 immunoprecipitates were phosphorylated by purified MEK1;
however, RSK3 kinase activity was unaffected. We conclude that 1) the
MEK1-MAPK signaling pathway is both necessary and sufficient for
in vivo growth factor-mediated activation of all three RSK
isoforms; 2) RSK isoforms differ with respect to growth factor
responsiveness and their physical association with MAPK; and 3)
formation of the MAPK·RSK complex is mediated by the RSK C
terminus.
Volume 271, Number 47,
Issue of November 22, 1996
pp. 29773-29779
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
,
and**
Department of Medicine, Beth Israel Hospital
and Harvard Medical School, Boston, Massachusetts 02215 and the
** Department of Molecular Endocrinology, Merck Research Laboratories,
Rahway, New Jersey 07065
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G.-Y. Wu, K. Deisseroth, and R. W. Tsien Activity-dependent CREB phosphorylation: Convergence of a fast, sensitive calmodulin kinase pathway and a slow, less sensitive mitogen-activated protein kinase pathway PNAS, February 27, 2001; 98(5): 2808 - 2813. [Abstract] [Full Text] [PDF]
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