Korean J Physiol Pharmacol.  2009 Oct;13(5):343-348. 10.4196/kjpp.2009.13.5.343.

Ser1778 of 53BP1 Plays a Role in DNA Double-strand Break Repairs

Affiliations
  • 1Department of Pharmacology, DNA Repair Research Center, Chosun University School of Medicine, Gwangju 501-759, Korea. shsfkys@chosun.ac.kr
  • 2Department of Life Science, College of Natural Science, Chung-Ang University, Seoul 156-756, Korea.
  • 3Division of Influenza and Respiratory Viruses, Center for Infectious Disease, National Institute of Health, Korea Center for Disease Control and Prevention, Seoul 122-701, Korea.
  • 4Department of Internal Medicine, Chosun University Hospital, Gwangju 501-717, Korea.

Abstract

53BP1 is an important genome stability regulator, which protects cells against double-strand breaks. Following DNA damage, 53BP1 is rapidly recruited to sites of DNA breakage, along with other DNA damage response proteins, including gamma-H2AX, MDC1, and BRCA1. The recruitment of 53BP1 requires a tandem Tudor fold which associates with methylated histones H3 and H4. It has already been determined that the majority of DNA damage response proteins are phosphorylated by ATM and/or ATR after DNA damage, and then recruited to the break sites. 53BP1 is also phosphorylated at several sites, like other proteins after DNA damage, but this phosphorylation is not critically relevant to recruitment or repair processes. In this study, we evaluated the functions of phosphor-53BP1 and the role of the BRCT domain of 53BP1 in DNA repair. From our data, we were able to detect differences in the phosphorylation patterns in Ser25 and Ser1778 of 53BP1 after neocarzinostatin-induced DNA damage. Furthermore, the foci formation patterns in both phosphorylation sites of 53BP1 also evidenced sizeable differences following DNA damage. From our results, we concluded that each phosphoryaltion site of 53BP1 performs different roles, and Ser1778 is more important than Ser25 in the process of DNA repair.

Keyword

53BP1; Phosphorylation; Nuclear foci; DSBs; DNA repair
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