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J. Biol. Chem., Vol. 275, Issue 31, 23549-23558, August 4, 2000
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From the RSKB, a 90-kDa ribosomal S6 protein kinase family
(RSK) member with two complete catalytic domains connected by a linker, is activated through p38- and ERK-mitogen-activated protein kinases. The N-terminal kinases of RSKs phosphorylate substrates; activation requires phosphorylation of linker and C-terminal kinase sites. Unlike
other RSKs, the activation loop phosphorylation sites of both catalytic
domains of RSKB, Ser196 and
Thr568, were required for activity. RSKB activation
depended on phosphorylation of linker Ser343 and
Ser360 and associated with phosphorylation of nonconserved
Ser347, but Ser347-deficient RSKB retained
partial activity. The known protein kinase A and protein kinase
C inhibitors, H89 and Ro31-8220, blocked RSKB activity. Treatment of
HeLa cells with tumor necrosis factor, epidermal growth factor,
phorbol 12-myristate 13-acetate, and ionomycin but not with insulin
resulted in strong activation of endogenous RSKB. High RSKB activity
and Ser347/Ser360 phosphorylation persisted for
3 h in tumor necrosis factor-treated cells, in contrast to the
short bursts of p38, ERK, and RSK1-3 activities. In conclusion, a
variety of stimuli induced phosphorylation and activation of RSKB
through both p38 and ERK pathways; the persistence of activation
indicated that RSKB selectively escaped cell mechanisms causing rapid
deactivation of upstream p38 and ERK and other RSKs.
Control Sites of Ribosomal S6 Kinase B and Persistent Activation
through Tumor Necrosis Factor*
,¶
Department PRPN and § Department
PRPV of F. Hoffmann-LaRoche, Ltd., CH-4070 Basel, Switzerland and the
¶ Department of Epidemiology and Public Health and Section of
Immunobiology, Yale University School of Medicine,
New Haven, Connecticut 06520-8034
*
The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Yale University
School of Medicine, Dept. of Epidemiology and Public Health, 60 College
St., P.O. Box 208034, New Haven, CT 06520-8034. Tel.: 203 785 7440;
Fax: 203 785 6130; E-mail: werner.lesslauer@yale.edu.
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