RNF111 ubiquitinates SUMOylated XPC

Stable Identifier
Reaction [transition]
Homo sapiens
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SUMOylated XPC is recognized by the SUMO-targeted ubiquitin ligase RNF111 (Arcadia) that, together with the E2 ubiquitin conjugating complex of UBE2N (UBC13) and UBE2V2 (MMS2), generates K63-linked polyubiquitin chains on XPC (Poulsen et al. 2013) to efficiently release XPC from UV lesions (van Cuijk et al. 2015). The release of K63-polyubiquitinated XPC occurs from GG-NER pre-incision complexes that contain TFIIH and XPA and promotes optimal access/binding of ERCC5 (XPG) endonuclease to the pre-incision complex (van Cuijk et al. 2015). Successful binding of ERCC5 endonuclease 3' to the damage facilitates binding of the ERCC1:ERCC4 (ERCC1:XPF) endonuclease and progression of the NER reaction.

Literature References
PubMed ID Title Journal Year
26151477 SUMO and ubiquitin-dependent XPC exchange drives nucleotide excision repair

Houtsmuller, AB, Lans, H, Sabatella, M, Poulsen, SL, Theil, AF, Janssens, RC, van Belle, GJ, Marteijn, JA, van Cuijk, L, Turkyilmaz, Y, Mailand, N, Vermeulen, W

Nat Commun 2015
23751493 RNF111/Arkadia is a SUMO-targeted ubiquitin ligase that facilitates the DNA damage response

Houtsmuller, AB, Poulsen, SL, Hansen, RK, Wikström, M, van Belle, GJ, Marteijn, JA, van Cuijk, L, Streicher, W, Choudhary, C, Bekker-Jensen, S, Mailand, N, Wagner, SA

J. Cell Biol. 2013
Catalyst Activity

ubiquitin protein ligase activity of RNF111 [nucleoplasm]

Orthologous Events
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