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Mammalian SUMO E3-ligases PIAS1 and PIAS4 promote responses to DNA double-strand breaks

Author

Listed:
  • Yaron Galanty

    (The Wellcome Trust and Cancer Research UK Gurdon Institute, University of Cambridge, Tennis Court Road, Cambridge CB2 1QN, UK)

  • Rimma Belotserkovskaya

    (The Wellcome Trust and Cancer Research UK Gurdon Institute, University of Cambridge, Tennis Court Road, Cambridge CB2 1QN, UK)

  • Julia Coates

    (The Wellcome Trust and Cancer Research UK Gurdon Institute, University of Cambridge, Tennis Court Road, Cambridge CB2 1QN, UK)

  • Sophie Polo

    (The Wellcome Trust and Cancer Research UK Gurdon Institute, University of Cambridge, Tennis Court Road, Cambridge CB2 1QN, UK)

  • Kyle M. Miller

    (The Wellcome Trust and Cancer Research UK Gurdon Institute, University of Cambridge, Tennis Court Road, Cambridge CB2 1QN, UK)

  • Stephen P. Jackson

    (The Wellcome Trust and Cancer Research UK Gurdon Institute, University of Cambridge, Tennis Court Road, Cambridge CB2 1QN, UK)

Abstract

SUMO modification and the response to DNA damage The occurrence of a double-strand break in DNA activates a complex series of events that recruit to the break many proteins involved in its repair. A number of these proteins are modified by addition of a small protein, SUMO; this modification is performed SUMO ligases. In this work, Jackson and colleagues show that two such ligases, PIAS1 and PIAS4, add various SUMOs onto DNA repair proteins at double-strand breaks. The PIAS ligases are recruited via their SAP domains, and their activity is required for effective repair. SUMOylation by PIAS1 and PIAS4 is also necessary for the further modification of certain repair factors by ubiquitin, a somewhat larger protein adduct related to SUMO. The successive SUMOylation and ubiquitylation of repair proteins regulates their targeting to, and repair of, DNA breaks.

Suggested Citation

  • Yaron Galanty & Rimma Belotserkovskaya & Julia Coates & Sophie Polo & Kyle M. Miller & Stephen P. Jackson, 2009. "Mammalian SUMO E3-ligases PIAS1 and PIAS4 promote responses to DNA double-strand breaks," Nature, Nature, vol. 462(7275), pages 935-939, December.
  • Handle: RePEc:nat:nature:v:462:y:2009:i:7275:d:10.1038_nature08657
    DOI: 10.1038/nature08657
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    Cited by:

    1. Joana S. Rodrigues & Miguel Chenlo & Susana B. Bravo & Sihara Perez-Romero & Maria Suarez-Fariña & Tomas Sobrino & Rebeca Sanz-Pamplona & Román González-Prieto & Manuel Narciso Blanco Freire & Ruben N, 2024. "dsRNAi-mediated silencing of PIAS2beta specifically kills anaplastic carcinomas by mitotic catastrophe," Nature Communications, Nature, vol. 15(1), pages 1-30, December.
    2. Jenny Kaur Singh & Rebecca Smith & Magdalena B. Rother & Anton J. L. Groot & Wouter W. Wiegant & Kees Vreeken & Ostiane D’Augustin & Robbert Q. Kim & Haibin Qian & Przemek M. Krawczyk & Román González, 2021. "Zinc finger protein ZNF384 is an adaptor of Ku to DNA during classical non-homologous end-joining," Nature Communications, Nature, vol. 12(1), pages 1-21, December.
    3. Laura A. Claessens & Matty Verlaan-de Vries & Ilona J. Graaf & Alfred C. O. Vertegaal, 2023. "SENP6 regulates localization and nuclear condensation of DNA damage response proteins by group deSUMOylation," Nature Communications, Nature, vol. 14(1), pages 1-19, December.

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