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J. Biol. Chem., Vol. 278, Issue 19, 17299-17306, May 9, 2003
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From the Institute of Molecular Medicine and Genetics and
Department of Radiology, Medical College of Georgia,
Augusta, Georgia 30912
Heat shock factor 1 (HSF1) regulates the rapid
and transient expression of heat shock genes in response to stress. The
transcriptional activity of HSF1 is tightly controlled, and
under physiological growth conditions, the HSF1 monomer is in a
heterocomplex with the molecular chaperone HSP90. Through unknown
mechanisms, transcriptionally repressed HSF1·HSP90
heterocomplexes dissociate following stress, which triggers HSF1
activation and heat shock gene transcription. Using a yeast two-hybrid
screening system, we have identified Ral-binding protein 1 (RalBP1) as
an additional HSF1-interacting protein. We show that RalBP1 and HSF1
interact in vivo, and transient cotransfection of HSF1
and RalBP1 into hsf1
HSF-1 Interacts with Ral-binding Protein 1 in a
Stress-responsive, Multiprotein Complex with HSP90 in
Vivo*
/ mouse embryo
fibroblasts represses HSP70 expression. Furthermore, transient
cotransfection of HSF1 and the constitutively active form of RalA
(RalA23V), an upstream activator of the RalBP1 signaling pathway,
increases the heat-inducible expression of HSP70, whereas the
dominant negative form (RalA28N) suppresses HSP70 expression. We
further find that 
-tubulin and HSP90 are also present in the RalBP1·HSF1 heterocomplexes in unstressed cells. Upon heat shock, the
Ral signaling pathway is activated, and the resulting RalGTP binds
RalBP1. Concurrently, HSF1 is activated, leaves the
RalBP1·HSF1·HSP90·-tubulin heterocomplexes, and translocates
into the nucleus, where it then activates transcription. In conclusion,
these observations reveal that the RalGTP signal transduction pathway
is critical for activation of the stress-responsive HSF1 and perhaps
HSP90 molecular chaperone system.
*
This work was supported by NCI, National Institutes of
Health, Grants CA62130 and CA85947 (to N. F. M.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Medical College of
Georgia, Institute of Molecular Medicine and Genetics, 1120 15th St.
CB2803, Augusta, Georgia 30912. Tel.: 706-721-8759; Fax: 706-721-8752;
E-mail: mivechi@immag.mcg.edu.
Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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