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J Biol Chem, Vol. 273, Issue 32, 20090-20095, August 7, 1998
From the Several protein kinases (e.g.
pp60src, v-Raf) exist in heterocomplexes with hsp90 and a
50-kDa protein that is the mammalian homolog of the yeast cell cycle
control protein Cdc37. In contrast, unliganded steroid receptors exist
in heterocomplexes with hsp90 and a tetratricopeptide repeat (TPR)
domain protein, such as an immunophilin. Although p50cdc37 and
TPR domain proteins bind directly to hsp90, p50cdc37 is not
present in native steroid receptor·hsp90 heterocomplexes. To obtain
some insight as to how v-Raf selects predominantly
hsp90·p50cdc37 heterocomplexes, rather than hsp90·TPR
protein heterocomplexes, we have examined the binding of
p50cdc37 to hsp90 and to Raf. We show that p50cdc37
exists in separate hsp90 heterocomplexes from the TPR domain proteins
and that intact TPR proteins compete for p50cdc37 binding to
hsp90 but a protein fragment containing a TPR domain does not. This
suggests that the binding site for p50cdc37 lies topologically
adjacent to the TPR acceptor site on the surface of hsp90. Also, we
show that p50cdc37 binds directly to v-Raf, with the catalytic
domain of Raf being sufficient. We propose that the combination of
exclusive binding of p50cdc37 versus a TPR domain
protein to hsp90 plus direct binding of p50cdc37 to Raf allows
the protein kinase to select for the dominant hsp90·p50cdc37
composition that is observed with a variety of protein kinase heterocomplexes immunoadsorbed from cytosols.
p50cdc37 Binds Directly to the Catalytic Domain of Raf
as Well as to a Site on hsp90 That Is Topologically Adjacent to the
Tetratricopeptide Repeat Binding Site
,
Department of Pharmacology, The University
of Michigan Medical School, Ann Arbor, Michigan 48109, the
§ Department of Physiology, Tufts University School of
Medicine, Boston, Massachusetts 02111, and the ¶ Vollum Institute,
Oregon Health Sciences University, Portland, Oregon 97201
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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