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J. Biol. Chem., Vol. 276, Issue 7, 4677-4682, February 16, 2001
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From the The chaperone activity of Hsp70 is influenced by
the activities of both positive and negative regulatory proteins. In
this study, we provide first time evidence for the stimulating effect of the Hsp70-interacting protein Hip on the chaperone activity in the
mammalian cytosol. Overexpressing Hip enhances the refolding of the
heat-inactivated reporter enzyme luciferase expressed in hamster lung
fibroblasts. Also, it protects luciferase from irreversible denaturation under conditions of ATP depletion. We demonstrate that
these stimulating actions depend on both the presence of the central
Hsp70-binding site and the amino-terminal homo-oligomerization domain
of Hip. The carboxyl terminus (amino acids 257-368) comprising the 7 GGMP repeats (Hsc70-like domain) and the Sti1p-like domain are
dispensable for the Hip-mediated stimulation of the cellular chaperone
activity. Bag-1, which inhibits the Hsp70 chaperone activity both
in vitro and in vivo, was found to compete with the stimulatory action of Hip. In cells overexpressing both Hip and
Bag-1, the inhibitory effects of Bag-1 were found to be dominant. Our
results reveal that in vivo a complex level of regulation of the cellular chaperone activity exists that not only depends on the
concentration of Hsp70 but also on the concentration, affinity, and
intracellular localization of positive and negative coregulators. As
the Hsp70 chaperone machine is also protective in the absence of ATP,
our data also demonstrate that cycling between an ATP/ADP-bound state
is not absolutely required for the Hsp70 chaperone machine to be active
in vivo.
Modulation of in Vivo HSP70 Chaperone Activity by Hip
and Bag-1*
,,,
Department of Radiation and Stress Cell
Biology, Faculty of Medical Sciences, University of Groningen,
9713 AV Groningen, The Netherlands, § Medical Radiology
Research Center, Obninsk 249020, Russia, and ¶ Institute for Cell
Biology, Rheinische Friedrich-Wilhelms-Universität Bonn, D-53121
Bonn, Germany
*
This work was supported by the Dutch Cancer Society NKB
Grant 95-1082 (to H. H. K.), a grant from the Netherlands Science Organization (NWO) (to A. E. K and H. H. K.), and a grant from the
German Science Foundation (to J. H.).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: Dept. of Radiation
and Stress Cell Biology, Faculty of Medical Sciences, University of
Groningen, A. Deusinglaan 1, 9713 AV Groningen, The Netherlands. Tel.:
31-50-3632903-2911; Fax: 31-50-3632913; E-mail:
h.h.kampinga@med.rug.nl.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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