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J. Biol. Chem., Vol. 279, Issue 10, 9321-9330, March 5, 2004

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Nek9, a Novel FACT-associated Protein, Modulates Interphase Progression^*

Bertrand Chin-Ming Tan and Sheng-Chung Lee¶||

From the Institutes of Molecular Medicine and Clinical Medicine, College of Medicine, National Taiwan University and ^¶Institute of Biological Chemistry, Academia Sinica, Taipei, Taiwan

The heterodimeric Spt16-Pob3/DUF/FACT complex is a class of chromatin structure modulators with important roles in replication and transcription. Although regarded as a transcription elongator for chromatin template, little is known about the mode of action and involvement in other molecular processes of the mammalian FACT. Here we report the identification of a novel interacting and functional partner of FACT, Nek9. Nek9 forms a stable, 600-kDa complex with FACT in the interphase nuclei. Its active form is characterized by phosphorylation-dependent electrophoretic mobility shift and phosphorylation at a conserved residue within the activation loop (Thr²¹⁰). When complexed with FACT, Nek9 exhibits markedly elevated phosphorylation on Thr²¹⁰. Cell cycle analysis on the Nek9^dsRNAi cells directly implicated Nek9 in maintaining proper G₁ and S progression, a role temporally correlated to the formation of a phospho-Nek9-FACT complex. Collectively, these observations provide evidence that Nek9, potentially as an active enzymatic partner of FACT, mediates certain FACT-associated cellular processes, which are ultimately essential for interphase progression.

Received for publication, October 20, 2003 , and in revised form, November 25, 2003.

^* This work was supported by National Science Council Grants NSC90-2321-B002-003 and the Institute of Biological Chemistry, Academia Sinica, Taiwan. 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: Institute of Molecular Medicine, School of Medicine, National Taiwan University, 7 Chung Shan South Rd., Taipei, Taiwan. Tel.: 886-2-2356-2982; Fax: 886-2-2321-0977; E-mail: slee{at}ccms.ntu.edu.tw.

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