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Originally published In Press as doi:10.1074/jbc.C100228200 on November 26, 2001

J. Biol. Chem., Vol. 277, Issue 4, 2381-2384, January 25, 2002
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ACCELERATED PUBLICATION
Critical Role of WW Domain Phosphorylation in Regulating Phosphoserine Binding Activity and Pin1 Function*

Pei-Jung LuDagger §§§, Xiao Zhen ZhouDagger §, Yih-Cherng LiouDagger ||, Joseph P. Noel**, and Kun Ping LuDagger **Dagger Dagger

From the Dagger  Cancer Biology Program, Division of Hematology/Oncology, Department of Medicine, Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, Massachusetts 02215, the §§ Institute of Biomedical Sciences, National Sun Yat-Sen University, 804 Kaohsiung, Taiwan, and the ** Structural Biology Laboratory, The Salk Institute, La Jolla, California 92037

Phosphoserine-binding modules help determine the specificity of signal transduction events. One such module, the group IV WW domain, plays an essential role in targeting the phosphorylation-specific prolyl isomerase Pin1 to its substrates. These modules require Ser/Thr phosphorylation of their ligands for binding activity. However, phosphorylation of these modules and its functional significance have not been described, nor is it known whether the function of Pin1 is regulated. Here we show that Pin1 WW domain is phosphorylated on Ser16 both in vitro and in vivo. Further, this phosphorylation regulates the ability of the WW domain to mediate Pin1 substrate interaction and cellular localization. Moreover, both Pin1 and WW domain mutants refractory to Ser16 phosphorylation act as dominant-negative mutants to induce mitotic block and apoptosis and increase multinucleated cells with 8 N DNA content. Thus, phosphorylation is a new mechanism critical for regulating WW domain phosphoserine binding activity and Pin1 function.

* This work was supported by National Institutes of Health Grants R01GM56230 and GM58556 (to K. P. L.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ These authors contributed equally to this work.

Fellow of the Leukemia and Lymphoma Society.

|| Fellow of the Canadian National Science and Engineering Research Council.

Dagger Dagger A Pew Scholar and a Leukemia and Lymphoma Society Scholar. To whom correspondence should be addressed: Beth Israel Deaconess Medical Center, 330 Brookline Ave., HIM 1047, Boston, MA 02215. Tel.: 617-667-4143; Fax: 617-667-0610; E-mail: klu@caregroup.harvard.edu.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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