The shieldin complex mediates 53BP1-dependent DNA repair.

ABSTRACT: 53BP1 is a chromatin-binding protein that regulates the repair of DNA double-strand breaks by suppressing the nucleolytic resection of DNA termini^1,2. This function of 53BP1 requires interactions with PTIP³ and RIF1^4-9, the latter of which recruits REV7 (also known as MAD2L2) to break sites^10,11. How 53BP1-pathway proteins shield DNA ends is currently unknown, but there are two models that provide the best potential explanation of their action. In one model the 53BP1 complex strengthens the nucleosomal barrier to end-resection nucleases^12,13, and in the other 53BP1 recruits effector proteins with end-protection activity. Here we identify a 53BP1 effector complex, shieldin, that includes C20orf196 (also known as SHLD1), FAM35A (SHLD2),

SUBMITTER: Noordermeer SM 

PROVIDER: S-EPMC6141009 | biostudies-literature | 2018 Aug

REPOSITORIES: biostudies-literature