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J. Biol. Chem., Vol. 279, Issue 48, 50157-50166, November 26, 2004

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p14 Arf Promotes Small Ubiquitin-like Modifier Conjugation of Werners Helicase^*

Yvonne L. Woods¶, Dimitris P. Xirodimas, Alan R. Prescott||, Alison Sparks, David P. Lane**, and Mark K. Saville

From the CR-UK Cell Transformation Research Group, Department of Surgery and Molecular Oncology, Ninewells Hospital and Medical School, Ninewells Avenue, Dundee DD1 9SYand ^||University of Dundee, MSI/WTB Complex, School of Life Sciences, Dow Street, Dundee DD1 5EH, United Kingdom

Here we demonstrate a novel p53-independent interaction between the nucleolar tumor suppressors, p14 Arf and Werners helicase (WRN). Binding of p14 Arf to WRN is multivalent and resembles the binding of p14 Arf to Mdm2. Residues 2–14 and 82–101 of p14 Arf and residues in the central region and C terminus of WRN have particular importance for binding. p14 Arf promotes small ubiquitin-like modifier (SUMO) modification of WRN in a synergistic manner with the SUMO-conjugating enzyme, UBCH9. p14 Arf causes redistribution of WRN within the nucleus, and this effect is reversed by expression of a SUMO-specific protease, thus implicating the SUMO conjugation pathway in WRN re-localization. We establish that the ability to promote SUMO conjugation is a general property of the p14 Arf tumor suppressor.

Received for publication, May 14, 2004 , and in revised form, August 17, 2004.

^* 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.

Recipient of a post-doctoral fellowship from Cancer Research UK.

^** Gibb fellow of Cancer Research UK.

^¶ To whom correspondence should be addressed. Tel.: 01382-496362; Fax: 01382-496361; E-mail: y.l.woods{at}dundee.ac.uk.

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