Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.


Sci. Signal., 4 December 2012
Vol. 5, Issue 253, p. ra88
[DOI: 10.1126/scisignal.2003485]


Editor's Summary

Hybrid Chains Mark the Spot
Posttranslational modifications play a key role in marking sites of DNA damage so that the DNA repair machinery can find the damaged area and effect repair. Guzzo et al. report a role for hybrid chains consisting of SUMO attached to a Lys63-linked diubiquitin as contributing to the recruitment of the protein RAP80, which in turn recruits the DNA repair protein BRCA1, to sites of damaged DNA. Knockdown of the E3 ligase RNF4, which synthesizes hybrid SUMO-ubiquitin linkages, prevented efficient recruitment of RAP80 and BRCA1 to sites of DNA damage induced by irradiation. This study defined a high-affinity interaction between a closely positioned pair of ubiquitin-interacting motifs and a SUMO-interacting motif in RAP80 that contributes to the recognition of sites of DNA damage.

Citation: C. M. Guzzo, C. E. Berndsen, J. Zhu, V. Gupta, A. Datta, R. A. Greenberg, C. Wolberger, M. J. Matunis, RNF4-Dependent Hybrid SUMO-Ubiquitin Chains Are Signals for RAP80 and Thereby Mediate the Recruitment of BRCA1 to Sites of DNA Damage. Sci. Signal. 5, ra88 (2012).

Read the Full Text

A SUMO-targeted ubiquitin ligase is involved in the degradation of the nuclear pool of the SUMO E3 ligase Siz1.
J. W. Westerbeck, N. Pasupala, M. Guillotte, E. Szymanski, B. C. Matson, C. Esteban, and O. Kerscher (2014)
Mol. Biol. Cell 25, 1-16
   Abstract »    Full Text »    PDF »
2012: Signaling Breakthroughs of the Year.
M. B. Yaffe and N. R. Gough (2013)
Science Signaling 6, eg1
   Abstract »    Full Text »    PDF »

To Advertise     Find Products

Science Signaling. ISSN 1937-9145 (online), 1945-0877 (print). Pre-2008: Science's STKE. ISSN 1525-8882