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A more recent version of this article appeared on March 5, 2004 Originally published In Press as doi:10.1074/jbc.M311477200 on December 2, 2003
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Papers In Press, published online ahead of print December 19, 2003
J. Biol. Chem, 10.1074/jbc.M311477200
Submitted on October 20, 2003
Revised on November 25, 2003
Accepted on December 1, 2003

Nek9, a novel FACT-associated protein, modulates interphase progression

Bertrand Chin-Ming Tan and Sheng-Chung Lee

Institute of Molecular Medicine, College of Medicine, National Taiwan University, Taipei, Taiwan 100

Corresponding Author: slee{at}ccms.ntu.edu.tw

The heterodimeric Spt16-Pob3/DUF/FACT complex is a class of chromatin structure modulator with important roles in replication and transcription. Although regarded as transcription elongator for chromatin template, little is known about mammalian FACT’s mode of action and involvement in other molecular processes. 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 Nek9dsRNAi 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.


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