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Cell Mol Life Sci. 2009 Jun;66(11-12):1840-9. doi: 10.1007/s00018-009-9152-0.

Protein kinase CK2 in health and disease: CK2: the kinase controlling the Hsp90 chaperone machinery.

Author information

1
Department of Cell and Developmental Biology, Graduate School of Biostudies, Kyoto University, Kitashirakawa Oiwake-cho, Sakyo-ku, Kyoto, 606 - 8502, Japan. ymiyata@lif.kyoto-u.ac.jp

Abstract

CK2 is a ubiquitous and essential protein kinase with pleiotropic substrates and function, but it remains unclear how, when, and where CK2 activity is regulated in cells. Hsp90 is a major molecular chaperone that is required for the folding and function of its client proteins. A complex containing Hsp90 and its client protein includes co-chaperones such as steroid hormone receptor-specific FKBP52 and signaling kinase-specific Cdc37. Co-chaperones work cooperatively with Hsp90 to stabilize client proteins and to keep them in a conformation amenable to activation under appropriate conditions. In this review, critical roles of CK2 in the regulation of the Hsp90-mediated chaperone system are described. CK2 phosphorylates and modulates Hsp90 and its co-chaperones FKBP52 and Cdc37. CK2-dependent phosphorylation of Cdc37 is essential for the chaperoning function of Hsp90-Cdc37 for multiple signaling protein kinases. The tumor kinome appears to become addicted to the Hsp90-Cdc37 chaperone system, thus, targeting Hsp90, Cdc37, and CK2 is a promising strategy for cancer treatment.

PMID:
19387550
DOI:
10.1007/s00018-009-9152-0
[Indexed for MEDLINE]

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