Roles of E3 ubiquitin ligase RNF168 as an adaptor molecule for histone H3 methylation

2015 Fiscal Year Final Research Report

• Project/Area Number: 25550028
• Research Category: Grant-in-Aid for Challenging Exploratory Research
• Allocation Type: Multi-year Fund
• Research Field: Risk sciences of radiation and chemicals
• Research Institution: Osaka University
• Principal Investigator: Nakada Shinichiro 大阪大学, 医学(系)研究科(研究院), 准教授 (70548528)
• Project Period (FY): 2013-04-01 – 2016-03-31
• Keywords: DNA修復 / DNA2本鎖切断

Outline of Final Research Achievements

53BP1 localizes to sites of DNA double-strand breaks (DSBs) and protects the DSB ends from degradation. Since the localization of 53BP1 to DSB sites depends on E3 ubiquitin ligase RNF168, we investigated the molecular mechanism how RNF168 regulates the 53BP1 accumulation at DSB sites. Our data suggest that RNF168 forms protein complex with BAT3 and DOT1L and these proteins also regulate the localization of 53BP1 to DSB sites. Even though other data implicate that contribution of the function of RNF168 as an adaptor is partial, RNF168 can works as an adaptor for the localization of DOT1L to DSB sites. Our data also suggest that RNF168 localizes to DSB sites by a mechanism that has not been reported yet.

Free Research Field

DNA修復