RNF8 binds phosphorylated MDC1 at DNA DSBs

Stable Identifier
Reaction [binding]
Homo sapiens
Locations in the PathwayBrowser
SVG |   | PPTX  | SBGN
Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout

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
Orthologous Events
Cite Us!