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, Mark K. Saville

    Research output: Contribution to journalArticle

    51 Citations (Scopus)

    Abstract

    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.
    Original languageEnglish
    Pages (from-to)50157-50166
    Number of pages10
    JournalJournal of Biological Chemistry
    Volume279
    Issue number48
    DOIs
    Publication statusPublished - 2004

    Fingerprint Dive into the research topics of 'p14 arf promotes small ubiquitin-like modifier conjugation of Werners helicase'. Together they form a unique fingerprint.

  • Cite this