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J Biol Chem, Vol. 273, Issue 45, 29417-29423, November 6, 1998
Activation of Nuclear Transcription
Factor-
B in Marrow Macrophages Is Mediated by c-Src Tyrosine
Phosphorylation of IB
,,,
From the Tumor necrosis factor- Department of Pathology, Washington
University School of Medicine, St. Louis, Missouri 63110 and ¶ CJF
INSERM 96-05, Faculty of Medicine Pasteur, 06107 Nice Cedex 2, France
(TNF) exerts its
transcriptional effects via activation of nuclear transcription
factor-
B (NF-B). NF-B is sequestered in the cytosol by
IB and, in most cells, released upon serine phosphorylation of
this inhibitory protein which then undergoes rapid,
ubiquitin-dependent degradation. In contrast, we find TNF
induction of NF-B in murine bone marrow macrophages (BMMs), is
mediated, by c-Src, in a cell, and cytokine specific manner. The
non-receptor tyrosine kinase is rapidly mobilized and activated upon
TNF exposure. Within the same time frame, TNF induced c-Src associates
with IB in a long lived complex. The proto-oncogene, when
associated with IB phosphorylates the inhibitory protein on
tyrosine 42. Consistent with the pivotal role played by c-Src in
TNF-induced IB tyrosine phosphorylation, NF-B activation, by
the cytokine, is markedly delayed and reduced in c-src
/
BMMs. Underscoring the physiological significance of c-Src activation of NF-B, TNF induction of IL-6, which is an NF-B mediated event, is substantially diminished in c-src/ BMMs.
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