In the absence of DNA damage, the ubiquitin ligase activity of UV-DDB complex is inhibited by association with the COP9 signalosome (CSN complex), which dissociates from the UV-DDB complex upon binding to damaged DNA (Groisman et al. 2003, Fischer et al. 2011). Ubiquitination of XPC by UV-DDB promotes XPC retention at GG-NER sites, while progressive autoubiquitination of UV-DDB promotes the dissociation of UV-DDB from the DNA and may act as an intracellular signal (Sugasawa et al. 2005). The UV-DDB complex also ubiquitinates histones H2A, H3 and H4, which may trigger chromatin remodeling at DNA damage site and regulate the accessibility of damaged DNA to repair factors (Kapetanaki et al. 2006, Wang et al. 2006).
Kapetanaki, MG, Bisi, DC, Hsieh, CL, Guerrero-Santoro, J, Levine, AS, Rapić-Otrin, V
Lingaraju, GM, Gut, H, Yasuda, T, Iwai, S, Thomä, NH, Sugasawa, K, Scrima, A, Fischer, ES, Cavadini, S, Böhm, K, Hanaoka, F, Wakasugi, M, Faty, M, Matsumoto, S
Okuda, Y, Mori, T, Tanaka, K, Saijo, M, Tanaka, K, Iwai, S, Matsuda, N, Sugasawa, K, Hanaoka, F, Nishi, R, Chu, G
Xiong, Y, Zhai, L, Zhang, Y, Wang, H, Tempst, P, Jackson, S, Joo, HY, Erdjument-Bromage, H, Xu, J
ubiquitin protein ligase activity of XPC:RAD23:CETN2:Distorted dsDNA:UV-DDB [nucleoplasm]
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