Association of RAD52 with the RPA complex at resected DNA DSBs

Stable Identifier
R-HSA-5693580
Type
Reaction [binding]
Species
Homo sapiens
Compartment
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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).

Literature References
PubMed ID Title Journal Year
12139939 Analysis of the human replication protein A:Rad52 complex: evidence for crosstalk between RPA32, RPA70, Rad52 and DNA

Jackson, D, Dhar, K, Wahl, JK, Wold, MS, Borgstahl, GE

J. Mol. Biol. 2002
12379650 Regulation of ionizing radiation-induced Rad52 nuclear foci formation by c-Abl-mediated phosphorylation

Kitao, H, Yuan, ZM

J. Biol. Chem. 2002
10921897 Precise binding of single-stranded DNA termini by human RAD52 protein.

Parsons, CA, Baumann, P, Van Dyck, E, West, SC

EMBO J 2000
8702565 Physical interaction between human RAD52 and RPA is required for homologous recombination in mammalian cells

Park, MS, Ludwig, DL, Stigger, E, Lee, SH

J. Biol. Chem. 1996
12750383 WRN interacts physically and functionally with the recombination mediator protein RAD52

Baynton, K, Otterlei, M, Bjørås, M, von Kobbe, C, Bohr, VA, Seeberg, E

J. Biol. Chem. 2003
21804533 Tyrosine phosphorylation enhances RAD52-mediated annealing by modulating its DNA binding

Honda, M, Okuno, Y, Yoo, J, Ha, T, Spies, M

EMBO J. 2011
18757400 BCR/ABL and other kinases from chronic myeloproliferative disorders stimulate single-strand annealing, an unfaithful DNA double-strand break repair

Cramer, K, Nieborowska-Skorska, M, Koptyra, M, Slupianek, A, Penserga, ET, Eaves, CJ, Aulitzky, W, Skorski, T

Cancer Res. 2008
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