RAD52 heptamers bind 3' overhanging ssDNA at resected DNA double-strand breaks (DSBs) by simultaneously interacting with the DNA and the RPA complex. The conformation of the RAD52-ssDNA complex is thought to place the ssDNA on an exposed surface of the ring, in a configuration that may promote the DNA-DNA annealing of complementary DNA strands (Parsons et al. 2000). The interaction with RPA is necessary for RAD52-mediated homology driven repair (Park et al. 1996, Jackson et al. 2002). Phosphorylation of RAD52 at tyrosine residue Y104 by ABL1 in response to ATM signaling increases the affinity of RAD52 for DNA (Kitao et al. 2002, Cramer et al. 2008, Honda et al. 2011). Long range resection, which results in the activation of ATR/CHEK1 signaling, is needed for RAD52-mediated single strand annealing (SSA). RAD52 function may be promoted by a direct interaction with WRN helicase which participates in long-range resection of DNA DSBs (Baynton et al. 2003).
Kitao, H, Yuan, ZM
Wold, MS, Jackson, D, Dhar, K, Wahl, JK, Borgstahl, GE
West, SC, Parsons, CA, Van Dyck, E, Baumann, P
Park, MS, Stigger, E, Lee, SH, Ludwig, DL
Otterlei, M, Baynton, K, Seeberg, E, von Kobbe, C, Bohr, VA, Bjørås, M
Spies, M, Ha, T, Honda, M, Yoo, J, Okuno, Y
Nieborowska-Skorska, M, Skorski, T, Slupianek, A, Penserga, ET, Aulitzky, W, Eaves, CJ, Koptyra, M, Cramer, K
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