Volume 22, No 8, Aug 2012

ISSN: 1001-0602 
EISSN: 1748-7838 2018 
impact factor 17.848* 
(Clarivate Analytics, 2019)

Volume 22 Issue 8, August 2012: 1221-1223

RESEARCH HIGHLIGHTS

K48-linked ubiquitination and protein degradation regulate 53BP1 recruitment at DNA damage sites

Frédérick A Mallette^1,2 and Stéphane Richard^1,2

¹Terry Fox Molecular Oncology Group and the Bloomfield Center for Research on Aging, Sir Mortimer B Davis Jewish General Hospital, Segal Cancer Centre, Lady Davis Institute for Medical Research, 3755 C魌e Ste-Catherine Road, Montr閍l, Qu閎ec, H3T 1E2, Canada;
²Departments of Medicine and Oncology, McGill University, Montr閍l, Qu閎ec, Canada Correspondence: Stéphane Richard,(stephane.richard@mcgill.ca)

Efficient DNA damage sensing and repair is crucial to preserve genomic integrity and failure to detect or repair DNA breaks can cause mutations, contributing to the formation of tumors. One key protein required for mediating DNA repair is the tumor suppressor 53BP1. Recent studies now demonstrate the crucial role of K48-linked ubiquitination and protein degradation for 53BP1 recruitment at sites of DNA damage.

Cell Research (2012) 22:1221-1223. doi:10.1038/cr.2012.58; published online 10 April 2012

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