Reactome | DNA Damage Recognition in GG-NER

DNA Damage Recognition in GG-NER

Stable Identifier

R-HSA-5696394

Type

Pathway

Species

Homo sapiens

Compartment

nucleoplasm

ReviewStatus

5/5

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In global genome nucleotide excision repair (GG-NER), the DNA damage is recognized by two protein complexes. The first complex consists of XPC, RAD23A or RAD23B, and CETN2. This complex probes the DNA helix and recognizes damage that disrupts normal Watson-Crick base pairing, which results in binding of the XPC:RAD23:CETN2 complex to the undamaged DNA strand. The second complex is a ubiquitin ligase UV-DDB that consists of DDB2, DDB1, CUL4A or CUL4B and RBX1. The UV-DDB complex is necessary for the recognition of UV-induced DNA damage and may contribute to the retention of the XPC:RAD23:CETN2 complex at the DNA damage site. The UV-DDB complex binds the damaged DNA strand (Fitch et al. 2003, Wang et al. 2004, Moser et al. 2005, Camenisch et al. 2009, Oh et al. 2011).

Literature References

PubMed ID	Title	Journal	Year
21388382	Nucleotide excision repair proteins rapidly accumulate but fail to persist in human XP-E (DDB2 mutant) cells Tamura, D, Emmert, S, Oh, KS, DiGiovanna, JJ, Kraemer, KH, Imoto, K	Photochem. Photobiol.	2011
19609301	Two-stage dynamic DNA quality check by xeroderma pigmentosum group C protein Clement, FC, Naegeli, H, Ferrando-May, E, Fei, J, Leitenstorfer, A, Träutlein, D, Camenisch, U	EMBO J.	2009
14742321	UV radiation-induced XPC translocation within chromatin is mediated by damaged-DNA binding protein, DDB2 Wang, QE, Zhu, Q, Wani, G, Chen, J, Wani, AA	Carcinogenesis	2004
15811629	The UV-damaged DNA binding protein mediates efficient targeting of the nucleotide excision repair complex to UV-induced photo lesions Alekseev, S, Yasui, A, Mullenders, LH, Volker, M, Moser, J, Kool, H, van Zeeland, AA, Vrieling, H	DNA Repair (Amst.)	2005
12944386	In vivo recruitment of XPC to UV-induced cyclobutane pyrimidine dimers by the DDB2 gene product Nakajima, S, Ford, JM, Yasui, A, Fitch, ME	J. Biol. Chem.	2003