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J. Biol. Chem., Vol. 279, Issue 31, 32592-32602, July 30, 2004

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Fbx7 Functions in the SCF Complex Regulating Cdk1-Cyclin B-phosphorylated Hepatoma Up-regulated Protein (HURP) Proteolysis by a Proline-rich Region^*

Jung-Mao Hsu, Yuan-Chii G. Lee, Chang-Tze R. Yu, and Chi-Ying F. Huang¶||**

From the Division of Molecular and Genomic Medicine, National Health Research Institutes, Taipei 115, Taiwan, the Graduate Institute of Medical Informatics, Taipei Medical University, Taipei 110, Taiwan, the ^¶Institute of Biotechnology in Medicine, National Yang-Ming University, Taipei 112, Taiwan, and the ^||Department of Computer Science and Information Engineering, National Taiwan University, Taipei 106, Taiwan, Republic of China

F-box proteins, components of SCF ubiquitin-ligase complexes, are believed to be responsible for substrate recognition and recruitment in SCF-mediated proteolysis. F-box proteins that have been identified to function in the SCF complexes to date mostly have substrate-binding motifs, such as WD repeats or leucine-rich repeats in their C termini. However, many F-box proteins lack recognizable substrate-binding modules; whether they can function in the SCF complexes remains unclear. We show here that Fbx7, an F-box protein without WD repeats and leucine-rich repeats, is required for the proteasome-mediated proteolysis of the hepatoma up-regulated protein (HURP). Depletion of Fbx7 by small interfering RNA leads to depression of HURP ubiquitination and accumulation of HURP abundance. In the SCF^Fbx7 complex, Fbx7 recruits HURP through its C-terminal proline-rich region in a Cdk1-cyclin B-phosphorylation dependent manner. Mutation of the multiple Cdk1-cyclin B phosphorylation sites on HURP or the proline-rich region of Fbx7 abolishes the association between Fbx7 and HURP. Thus, Fbx7 is a functional adaptor of the SCF complex with a proline-rich region as the substrate-binding module. In addition to Fbx7, data base analyses reveal two putative mammalian proline-rich region-containing F-box proteins, KIAA1783 and RIKEN cDNA 2410015K21. Taken together, these findings further expound the diverse substrate-recognition abilities of the SCF complexes.

Received for publication, May 4, 2004

^* This work was supported by a grant from the National Health Research Institutes. 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.

The on-line version of this article (available at http://www.jbc.org)contains Figs. S1-S3.

^** To whom correspondence should be addressed: Division of Molecular and Genomic Medicine, National Health Research Institutes, 128, Sec. 2, Academia Rd., Taipei 115, Taiwan, Republic of China. Tel.: 886-226534401 (ext. 6560); Fax: 886-227890484; E-mail: chiying{at}nhri.org.tw.

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