Reactome | RNF8 binds phosphorylated MDC1 at DNA DSBs

RNF8 binds phosphorylated MDC1 at DNA DSBs

Stable Identifier

R-HSA-5682588

Type

Reaction [binding]

Species

Homo sapiens

Compartment

nucleoplasm

ReviewStatus

5/5

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RNF8 binds phosphorylated MDC1 at DNA DSBs

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RNF8 is an E3 ubiquitin ligase that, through its FHA domain, binds MDC1 phosphorylated at T-Q-X-F (Thr-Gln-X-Phe) sites by ATM. The phosphorylation of at least four T-Q-X-F sites of MDC1 (T699, T719, T752, T765) increases RNF8 binding to MDC1 (Kolas et al. 2007). RNF8 functions as a homodimer formed by interactions of the RNF8 coiled-coil domains (Cambell et al. 2012).

Literature References

PubMed ID	Title	Journal	Year
18006705	Orchestration of the DNA-damage response by the RNF8 ubiquitin ligase Jackson, SP, Thomson, TM, Pelletier, L, Chapman, JR, Durocher, D, Panier, S, Mendez, M, Wildenhain, J, Nakada, S, Kolas, NK, Chahwan, R, Sweeney, FD, Ylanko, J	Science	2007
22589545	Molecular insights into the function of RING finger (RNF)-containing proteins hRNF8 and hRNF168 in Ubc13/Mms2-dependent ubiquitylation Campbell, SJ, Neculai, D, Leung, CC, Glover, JN, Dhe-Paganon, S, Hodge, CD, Edwards, RA	J. Biol. Chem.	2012