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J Biol Chem, Vol. 273, Issue 29, 18640-18646, July 17, 1998
From the Heat shock factor 1 (HSF1) is the key
transcriptional regulator of the heat shock genes that protect cells
from environmental stress. However, because heat shock gene expression
is deleterious to growth and development, we have examined mechanisms
for HSF1 repression at growth temperatures, focusing on the role of
phosphorylation. Mitogen-activated protein kinases (MAPKs) of the ERK
family phosphorylate HSF1 and represses transcriptional function. The
mechanism of repression involves initial phosphorylation by MAP kinase
on serine 307, which primes HSF1 for secondary phosphorylation by
glycogen synthase kinase 3 on a key residue in repression (serine 303). In vivo expression of glycogen synthase kinase 3 (
Transcriptional Activity of Heat Shock Factor 1 at
37 oC Is Repressed through Phosphorylation on Two Distinct
Serine Residues by Glycogen Synthase Kinase 3
and Protein
Kinases C and C
,,
,, and
Department of Adult Oncology, Dana Farber
Cancer Institute and Joint Center for Radiation Therapy, Harvard
Medical School, Boston, Massachusetts 02115 and the CNRS
EP 560, Institut Pasteur de Lille, 1 Rue
Calmette-BP 245, 59021 Lille Cedex, France
or
) thus represses HSF1 through phosphorylation of serine 303. HSF1 is also phosphorylated by MAPK in vitro on a second residue
(serine 363) adjacent to activation domain 1, and this residue is
additionally phosphorylated by protein kinase C. In vivo,
HSF1 is repressed through phosphorylation of this residue by protein
kinase C or -
but not MAPK. Regulation at 37 °C, therefore,
involves the action of three protein kinase cascades that repress HSF1
through phosphorylation of serine residues 303, 307, and 363 and may
promote growth by suppressing the heat shock response.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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