Reactome | POLI simultaneously binds REV1 and monoUb:K164-PCNA at damaged DNA

POLI simultaneously binds REV1 and monoUb:K164-PCNA at damaged DNA

Stable Identifier

R-HSA-5656105

Type

Reaction [binding]

Species

Homo sapiens

Compartment

nucleoplasm

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POLI simultaneously binds REV1 and monoUb:K164-PCNA at damaged DNA

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DNA polymerase iota (POLI) is recruited to DNA damage sites through its interaction with PCNA and REV1. POLI has a functional PIP box in the C-terminus and two ubiquitin binding motifs (UBMs). The PIP box and UBMs are responsible for POLI binding to monoubiquitinated PCNA (MonoUb:K164-PCNA) (Bienko et al. 2005, Haracska et al. 2005, Bomar et al. 2010). The interaction between POLI and the C-terminus of REV1 is evolutionarily conserved (Kosarek et al. 2003, Guo et al. 2003, Ohashi et al. 2004). Since REV1 and POLI likely cooperate in the bypass of bulky DNA lesions (Yang et al. 2003) and the DNA polymerase zeta complex (POLZ) is needed for extension of nucleotides incorporated by POLI (Johnson et al. 2000), it is plausible that POLI forms a quaternary complex with REV1 and POLZ, as shown for POLK and proposed for other Y family DNA polymerases (Xie et al. 2012).

Literature References

PubMed ID	Title	Journal	Year
10984059	Eukaryotic polymerases iota and zeta act sequentially to bypass DNA lesions Johnson, RE, Haracska, L, Washington, MT, Prakash, L, Prakash, S	Nature	2000
15189446	Interaction of hREV1 with three human Y-family DNA polymerases Murakumo, Y, Akagi, J, Kanjo, N, Hanaoka, F, Ohmori, H, Ohashi, E, Masutani, C	Genes Cells	2004
14657033	Mouse Rev1 protein interacts with multiple DNA polymerases involved in translesion DNA synthesis Masuda, Y, Friedberg, EC, Zhou, J, Fischhaber, PL, Guo, C, Kamiya, K, Kisker, C, Luk-Paszyc, MJ	EMBO J.	2003
15657443	A single domain in human DNA polymerase iota mediates interaction with PCNA: implications for translesion DNA synthesis Johnson, RE, Haracska, L, Hurwitz, J, Acharya, N, Prakash, L, Unk, I, Prakash, S	Mol. Cell. Biol.	2005
12584190	Mammalian translesion DNA synthesis across an acrolein-derived deoxyguanosine adduct. Participation of DNA polymerase eta in error-prone synthesis in human cells Miller, H, Moriya, M, Yang, IY, Wang, Z, Frank, EG, Hanaoka, F, Ohmori, H	J. Biol. Chem.	2003
20159559	Unconventional ubiquitin recognition by the ubiquitin-binding motif within the Y family DNA polymerases iota and Rev1 D'Souza, S, Bomar, MG, Zhou, P, Walker, GC, Dikic, I, Bienko, M	Mol. Cell	2010
18242152	Comparative analysis of in vivo interactions between Rev1 protein and other Y-family DNA polymerases in animals and yeasts D'Souza, S, Koonin, EV, Friedberg, EC, Woodruff, RV, Guo, C, Walker, GC, Kosarek, JN, Rivera-Begeman, A	DNA Repair (Amst.)	2008
16357261	Ubiquitin-binding domains in Y-family polymerases regulate translesion synthesis Hofmann, K, Crosetto, N, Green, CM, Lehmann, AR, Coull, B, Zapart, G, Peter, M, Kannouche, P, Rudolf, F, Wider, G, Dikic, I, Bienko, M	Science	2005