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B
and
Stimulates Its Degradation in Vitro
(Received for publication, January 3, 1997, and in revised form, May 20, 1997)
,
From the Nuclear factor University of Colorado Health Sciences
Center, Department of Pharmacology, School of Medicine, Denver,
Colorado 80262 and the ¶ Gladstone Institute of Virology and
Immunology and Departments of Medicine and Microbiology and
Immunology, University of California, San Francisco, San Francisco
General Hospital, San Francisco, California 94141-9100
B (NF-B) is a eukaryotic
member of the Rel family of transcription factors whose biological
activity is post-translationally regulated by its assembly with various
ankyrin-rich cytoplasmic inhibitors, including IB
. Expression of
NF-B in the nucleus occurs after signal-induced phosphorylation,
ubiquitination, and proteasome-mediated degradation of IB. The
induced proteolysis of IB unmasks the nuclear localization signal
within NF-B, allowing its rapid migration into the nucleus, where it
activates the transcription of many target genes. At present, the
identity of the IB kinase(s) that triggers the first step in
IB degradation remains unknown. We have investigated the
potential function of the 90-kDa ribosomal S6 kinase, or
pp90rsk, as a signal-inducible IB kinase.
pp90rsk lies downstream of mitogen-activated protein (MAP)
kinase in the well characterized Ras-Raf-MEK-MAP kinase pathway that is induced by various growth factors and phorbol ester. We now show that
pp90rsk, but not pp70S6K or MAP kinase,
phosphorylates the regulatory N terminus of IB principally on
serine 32 and triggers effective IB degradation in
vitro. When co-expressed in vivo in COS cells,
IB and pp90rsk readily assemble into a complex that
is immunoprecipitated with antibodies specific for either partner.
While phorbol 12-myristate 13-acetate produced rapid activation of
pp90rsk, in vivo, other potent NF-B
inducers, including tumor necrosis factor and the Tax
transactivator of human T-cell lymphotrophic virus, type I, failed to
activate pp90rsk. These data suggest that more than a
single IB kinase exists within the cell and that these IB
kinases are differentially activated by different NF-B inducers.
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M. Hinz, D. Krappmann, A. Eichten, A. Heder, C. Scheidereit, and M. S |
