E3 ubiquitin-protein ligase RNF169

Definition:

Probable E3 ubiquitin-protein ligase that acts as a regulator of double-strand breaks (DSBs) repair following DNA damage. Functions in a non-canonical fashion to harness RNF168-mediated protein recruitment to DSB-containing chromatin, thereby contributing to regulation of DSB repair pathway utilization. Once recruited to DSB repair sites by recognizing and binding ubiquitin catalyzed by RNF168, competes with TP53BP1 and BRCA1 for association with RNF168-modified chromatin, thereby favouring homologous recombination repair (HRR) and single-strand annealing (SSA) instead of non-homologous end joining (NHEJ) mediated by TP53BP1. E3 ubiquitin-protein ligase activity is not required for regulation of DSBs repair.

References:

[1]. Liwei An, et al. RNF169 limits 53BP1 deposition at DSBs to stimulate single-strand annealing repair. Proc Natl Acad Sci U S A. 2018 Aug 28;115(35):E8286-E8295. [Content Brief]

[2]. Maria Poulsen, et al. Human RNF169 is a negative regulator of the ubiquitin-dependent response to DNA double-strand breaks. J Cell Biol. 2012 Apr 16;197(2):189-99. [Content Brief]

[3]. Jie Chen, et al. Ring finger protein RNF169 antagonizes the ubiquitin-dependent signaling cascade at sites of DNA damage. J Biol Chem. 2012 Aug 10;287(33):27715-22. [Content Brief]

[4]. Stephanie Panier, et al. Tandem protein interaction modules organize the ubiquitin-dependent response to DNA double-strand breaks. Mol Cell. 2012 Aug 10;47(3):383-95. [Content Brief]

[5]. Vijay R Menon, et al. DYRK1A regulates the recruitment of 53BP1 to the sites of DNA damage in part through interaction with RNF169. Cell Cycle. 2019 Mar;18(5):531-551. [Content Brief]

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