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(Received for publication, December 4, 1996)
From the Departments of Hepatoma Hep3B cell lines stably expressing a
temperature-sensitive p53 species (p53-Val-135) displayed a reduced
response to interleukin-6 (IL-6) when cultured at the wild-type (wt)
p53 temperature (Wang, L., Rayanade, R., Garcia, D., Patel, K., Pan, H., and Sehgal, P. B. (1995) J. Biol. Chem. 270, 23159-23165). We now report that in such cultures IL-6 caused a rapid
(20-30 min) and marked loss of cellular immunostaining for STAT3 and STAT5, but not for STAT1. The loss of STAT3 and STAT5 immunostaining was transient (lasted 120 min) and tyrosine
kinase-dependent, and even though the loss was blocked by
the proteasome inhibitors MG132 and lactacystin it was not accompanied
by changes in cellular levels of STAT3 and STAT5 proteins suggesting
that IL-6 triggered a rapid masking but not degradation of these
transcription factors. STAT3 and STAT5 masking was accompanied by a
reduction in IL-6-induced nuclear DNA-binding activity. The data
suggest that p53 may influence Jak-STAT signaling through a novel
indirect mechanism involving a wt p53-dependent gene
product which upon cytokine addition is activated into a
"STAT-masking factor" in a proteasome-dependent step.
Volume 272, Number 8,
Issue of February 21, 1997
pp. 4659-4662
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
COMMUNICATION:
,
,
,§
,
,
and**
Cell Biology & Anatomy,
§ Ophthalmology, and ** Medicine, New York Medical College,
Valhalla, New York 10595, ¶ The Kitasato Institute, 9-1 Shirokane
5-Chome, Minato-ku, Tokyo 108, Japan, and the 
Public Health
Research Institute, New York, New York 10016
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