TFIIH binds GG-NER site to form a verification complex

Stable Identifier
Reaction [binding]
Homo sapiens
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Transcription factor II H (TFIIH) complex is recruited to DNA damage sites after the damage is recognized by the XPC:RAD23:CETN2 complex and the UV-DDB complex (DDB1:DDB2) (Volker et al. 2001, Araujo and Wood 1999).

TFIIH consists of ten subunits organized into a ring-like structure (Schultz et al. 2000). The TFIIH core, also forming a ring-like structure, includes a DNA helicase ERCC3 (XPB), GTF2H1 (BTF2-p62), GTF2H2 (BTF2-p44), GTF2H3 (BTF2-p34) and GTF2H4 (BTF2-p52). GTF2H4 directly interacts with ERCC3 and anchors it to the TFIIH complex (Jawhari et al. 2002). Another DNA helicase, ERCC2 (XPD) is anchored to the TFIIH complex by binding to the GTF2H2 subunit (Coin et al. 1998). The CDK-activating kinase (CAK) complex, consisting of CCNH (cyclin H), CDK7 and MNAT1 (MAT1) is included in the TFIIH complex through an interaction with ERCC2 (Reardon et al. 1996, Rossignol et al. 1997). The tenth subunit, GTF2H5 (TTDA, TFB5, BTF2-p5) is important for the stability of the TFIIH complex (Giglia-Mari et al. 2004). The TFIIH complex binds the DNA damage site after XPC:RAD23:CETN2 complex recognizes the damage (Volker et al. 2001, Riedl et al. 2003), and the ERCC3 and GTF2H1 subunits of TFIIH directly interact with XPC (Yokoi et al. 2003).

Literature References
PubMed ID Title Journal Year
14517266 The comings and goings of nucleotide excision repair factors on damaged DNA

Riedl, T, Egly, JM, Hanaoka, F

EMBO J. 2003
9771713 Mutations in the XPD helicase gene result in XP and TTD phenotypes, preventing interaction between XPD and the p44 subunit of TFIIH

Fribourg, S, Coin, F, Egly, JM, Rodolfo, C, Pedrini, AM, Marinoni, JC

Nat. Genet. 1998
10734143 The xeroderma pigmentosum group C protein complex XPC-HR23B plays an important role in the recruitment of transcription factor IIH to damaged DNA

Yokoi, M, Masutani, C, Maekawa, T, Sugasawa, K, Hanaoka, F, Ohkuma, Y

J. Biol. Chem. 2000
8692841 Isolation and characterization of two human transcription factor IIH (TFIIH)-related complexes: ERCC2/CAK and TFIIH

Hurwitz, J, Reardon, JT, Pan, ZQ, Sancar, A, Ge, H, Gibbs, E

Proc. Natl. Acad. Sci. U.S.A. 1996
11511374 Sequential assembly of the nucleotide excision repair factors in vivo.

van Zeeland, AA, Mullenders, LH, Vermeulen, W, van Driel, R, Karmakar, P, van Hoffen, A, Schul, W, Volker, M, Hoeijmakers, JH, Moné, MJ

Mol Cell 2001
9130708 Substrate specificity of the cdk-activating kinase (CAK) is altered upon association with TFIIH

Egly, JM, Kolb-Cheynel, I, Rossignol, M

EMBO J. 1997
25154395 Sequential and ordered assembly of a large DNA repair complex on undamaged chromatin

Alekseev, S, Ziani, S, Coin, F, Egly, JM, Soutoglou, E, Nagy, Z

J. Cell Biol. 2014
10526214 Protein complexes in nucleotide excision repair.

Wood, RD, Araujo, SJ

Mutat Res 1999
11007478 Molecular structure of human TFIIH

Fribourg, S, Schultz, P, Egly, JM, Moras, D, Mallouh, V, Poterszman, A

Cell 2000
15220921 A new, tenth subunit of TFIIH is responsible for the DNA repair syndrome trichothiodystrophy group A

Aebersold, R, Wijgers, N, Raams, A, Theil, A, Coin, F, Egly, JM, Hoogstraten, D, Botta, E, Stefanini, M, Giglia-Mari, G, Hoeijmakers, JH, van der Spek, PJ, Argentini, M, Jaspers, NG, Ranish, JA, Vermeulen, W

Nat. Genet. 2004
12080057 p52 Mediates XPB function within the transcription/repair factor TFIIH

Moras, D, Dubaele, S, Lamour, V, Poterszman, A, Coin, F, Jawhari, A, Egly, JM, Lainé, JP

J. Biol. Chem. 2002
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