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Originally published In Press as doi:10.1074/jbc.M404107200 on May 4, 2004

J. Biol. Chem., Vol. 279, Issue 29, 30662-30669, July 16, 2004
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Structural Basis of Membrane Targeting by the Phox Homology Domain of Cytokine-independent Survival Kinase (CISK-PX)*

Yi Xing{ddagger}, Dan Liu§, Rongguang Zhang¶, Andrzej Joachimiak¶, Zhou Songyang§, and Wenqing Xu{ddagger}||

From the {ddagger}Department of Biological Structure, University of Washington, Seattle, Washington 98195-7420, the §Verna and Marrs Mclean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, Texas 77030, and the Bioscience Division/Structural Biology Center, Argonne National Laboratory, Argonne, Illinois 60439

The cytokine-independent survival kinase (CISK) in the serum and glucocorticoid-regulated kinase family plays an important role in mediating cell growth and survival. N-terminal to its catalytic kinase domain, CISK contains a phox homology (PX) domain, a phosphoinositide-binding motif that directs the membrane localization of CISK and regulates CISK activity. We have determined the crystal structures of the mouse CISK-PX domain to unravel the structural basis of membrane targeting of CISK. In addition to the specific interactions conferred by the phosphoinositide-binding pocket, the structure suggests that a hydrophobic loop region and a hydrophilic {beta}-turn contribute to the interactions with the membrane. Furthermore, biochemical studies reveal that CISK-PX dimerizes in the presence of the linker between the PX domain and kinase domain, suggesting a multivalent mechanism in membrane localization of CISK.

Received for publication, April 13, 2004

* This work was supported in part by a New Investigator award (to W. X.) from the Diabetes Endocrinology Research Center at the University of Washington and in part by the U. S. Department of Energy, Office of Biological and Environmental Research under Contract W-31-109-Eng-38 (to A. J.) and by National Institutes of Health Grants CA84208 and GM69572 (to Z. S.). The costs of publication of this article were defrayed in part by the payment of page charges. This 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 Biological Structure, University of Washington, 1959 NE Pacific St., Seattle, WA 98195-7420. Tel.: 206-221-5609; Fax: 206-543-1524; E-mail: wxu{at}u.washington.edu.


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