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J Biol Chem, Vol. 274, Issue 46, 32631-32637, November 12, 1999
(HIF-1) and Enhance the
Transcriptional Activity of HIF-1
From the Institute of Signaling, Developmental Biology and Cancer
Research, UMR CNRS 6543, Centre Antoine Lacassagne, 33 Avenue
Valombrose, 06189 Nice, France
Hypoxia-inducible factor-1 (HIF-1) controls the
expression of a number of genes such as vascular endothelial growth
factor and erythropoietin in low oxygen conditions. However, the
molecular mechanisms that underlie the activation of the limiting
subunit, HIF-1
, are still poorly resolved. Results showing that
endogenous HIF-1 migrated 12 kDa higher than in vitro
translated protein led us to evaluate the possible role of
phosphorylation on this phenomenon. We report here that HIF-1 is
strongly phosphorylated in vivo and that phosphorylation is
responsible for the marked differences in the migration pattern of
HIF-1. In vitro, HIF-1 is phosphorylated by p42 and
p44 mitogen-activated protein kinases (MAPKs) and not by p38 MAPK or
c-Jun N-terminal kinase. Interestingly, p42/p44 MAPK stoichiometrically
phosphorylate HIF-1 in vitro, as judged by a complete
upper shift of HIF-1. More importantly, we demonstrate that
activation of the p42/p44 MAPK pathway in quiescent cells induced the
phosphorylation and shift of HIF-1, which was abrogated in presence
of the MEK inhibitor, PD 98059. Finally, we found that in a vascular
endothelial growth factor promoter mutated at sites previously shown to
be MAPK-sensitive (SP1/AP2-88-66 site), p42/p44 MAPK activation is
sufficient to promote the transcriptional activity of HIF-1. This
interaction between HIF-1 and p42/p44 MAPK suggests a cooperation
between hypoxic and growth factor signals that ultimately leads to the increase in HIF-1-mediated gene expression.
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