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J. Biol. Chem., Vol. 280, Issue 17, 17235-17242, April 29, 2005

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Binding of HTm4 to Cyclin-dependent Kinase (Cdk)-associated Phosphatase (KAP)·Cdk2·Cyclin A Complex Enhances the Phosphatase Activity of KAP, Dissociates Cyclin A, and Facilitates KAP Dephosphorylation of Cdk2^*

From the ^aDepartment of Nutrition, Kyushu Women's University, Jiyugaoka 1-1, Kitakyushushi 807-8586, Japan, the ^cDepartment of Medicine, Beth Israel Deaconess Medical Center, and ⁱDepartment of Medicine, Children's Hospital, Harvard Medical School, Boston, Massachusetts 02215, ^dDepartment of Internal Medicine, Fukuoka Dental School, Tamura, Sawaraku 2-15-1, 814-0193 Fukuoka, Japan, ^eMedical Institute of Bioregulation, Kyushu University, 3-1-1 Maidashi, Higashi-ku, Fukuoka, Fukuoka 812-8582, Japan, ^fQueen's Center for Biomedical Research, Queen's Medical Center, Honolulu, Hawaii 96813, ^gDepartment of Health Promotion and Human Behavior, Kyoto University Graduate School of Public Health, Kyoto 606-8501, Japan, and ^hRIKEN SNP Typing Center, Shirokanedai 4-6-1, Tokyo 108-8639, Japan

Cyclin-dependent kinase 2 (cdk2) activation requires phosphorylation of Thr¹⁶⁰ and dissociation from cyclin A. The T-loop of cdk2 contains a regulatory phosphorylation site at Thr¹⁶⁰. An interaction between cdc-associated phosphatase (KAP) and cdk2 compromises the interaction between cdk2 and cyclin A, which permits access of KAP, a Thr¹⁶⁰-directed phosphatase, to its substrate, cdk2. We have reported that KAP is bound and activated by a nuclear membrane protein, HTm4. Here, we present in vitro data showing the direct interaction between the HTm4 C terminus and KAP Tyr¹⁴¹. We show that this interaction not only facilitates access of KAP to Thr¹⁶⁰ and accelerates KAP kinetics, but also forces exclusion of cyclin A from the KAP·cdk2 complex.

Received for publication, November 30, 2004 , and in revised form, January 7, 2005.

^* This work was supported by Grant AI 43663 from the NIAID, National Institutes of Health, Grant RSG-01-241-01-LIB from the American Cancer Society (to C. N. A.), by grant-in-aid for Exploratory Research MEXT 15659112 from the Ministry of Education, Culture, Sports, Science and Technology of Japan, and by the Adra family. 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.

^b These authors contributed equally to this work.

^j To whom correspondence should be addressed: Dept. of Medicine, Harvard Medical School, Beth Israel Deaconess Medical Center, 99 Brookline Ave., Boston, MA 02215. Tel.: 617-667-3766; Fax: 617-975-7905; E-mail: cadra{at}caregroup.harvard.edu.

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