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Papers In Press, published online ahead of print March 21, 2006
J. Biol. Chem, 10.1074/jbc.M512613200
Submitted on November 28, 2005
Accepted on March 21, 2006

Hsp90 recognizes a common surface on client kinases

Ami Citri, Daniel Harari, Galit Shochat, Parameswaran Ramakrishnan, Judith Gan, Miriam Eisenstein, Adi Kimchi, David Wallach, Shmuel Pietrokovski, and Yosef Yarden

Biological Regulation, The Weizmann Institute of Science, Rehovot 76100

Corresponding Author: yosef.yarden{at}weizmann.ac.il

Hsp90 is a highly abundant chaperone, whose clientele includes hundreds of cellular proteins, many of which are central players in key signal transduction pathways, and the majority of which are protein kinases. In light of the variety of Hsp90 clientele, the mechanism of selectivity of the chaperone towards its client proteins is a major open question. Focusing on human kinases, we demonstrate that the chaperone recognizes a common surface in the amino-terminal lobe of kinases from diverse families, including two newly identified clients, NIK and DAPK, and the oncoprotein HER2/ErbB-2. Surface electrostatics determine the interaction with the Hsp90 chaperone complex, such that introduction of a negative charge within this region disrupts recognition. Compiling information on the Hsp90 dependence of 105 protein kinases, including 16 kinases whose relationship to Hsp90 is first examined in this study, reveals that surface features, rather than a contiguous amino-acid sequence, define the capacity of the Hsp90 chaperone machine to recognize client kinases. Analyzing Hsp90 regulation of two major signaling cascades, the MAP-kinase and PI-3 kinase, leads us to propose that the selectivity of the chaperone to specific kinases is functional, namely: Hsp90 controls kinases that function as hubs, integrating multiple inputs. These lessons bear significance to pharmacological attempts to target the chaperone in human pathologies, such as cancer.


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