POLH binds monoUb:K164-PCNA at damaged TT-CPD-DNA template

Stable Identifier
Reaction [binding]
Homo sapiens
Binding of Pol eta to lesioned DNA template
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DNA polymerase eta (POLH) belongs to Y family of DNA polymerases. POLH binds PCNA monoubiquitinated at lysine K164 by the RAD18:UBE2B (RAD18:RAD6) or RBX1:CUL4:DDB1:DTL complexes in response to DNA damage. POLH C-terminus contains a conserved PCNA interaction motif, while the catalytic domain of POLH contains a conserved monoubiquitin binding motif. POLH is most efficient in recognition and repair of thymine-thymine cyclobutane pyrimidine dimers (TT-CPD) induced by UV-mediated DNA damage (Masutani et al. 2000, Kannouche et al. 2004)

Literature References
PubMed ID Title Journal Year
15149598 Interaction of human DNA polymerase eta with monoubiquitinated PCNA: a possible mechanism for the polymerase switch in response to DNA damage

Kannouche, PL, Wing, J, Lehmann, AR

Mol. Cell 2004
10856253 Mechanisms of accurate translesion synthesis by human DNA polymerase eta.

Masutani, C, Kusumoto, R, Iwai, S, Hanaoka, F

EMBO J 2000
Participant Of
This event is regulated
Negatively by
Orthologous Events
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