Formation of BRCA1-A complex at DNA DSBs

Stable Identifier
R-HSA-5683385
Type
Reaction [binding]
Species
Homo sapiens
Compartment
nucleoplasm
ReviewStatus
5/5
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Formation of BRCA1-A complex at DNA DSBs
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A DNA damage-independent phosphorylation of FAM175A (Abraxas) serine residue S406 creates a pS-X-X-F (phospho-Ser-X-X-Phe) motif that binds BRCT repeats of BRCA1. The BRCA1 cancer predisposing mutation M1775R (Met1775Arg) inhibits BRCA1 binding to FAM175A. FAM175A interaction with UIMC1 (RAP80) enables BRCA1 recruitment to DNA double-strand breaks (DSBs) (Wang et al. 2007). In addition to BRCA1, FAM175A also interacts with BRCC3 (BRCC36) (Wang et al. 2007, Hu et al. 2011) and BABAM1 (MERIT40, NBA1) (Vikrant et al. 2014). BABAM1 simultaneously interacts with BRE (BRCC45) (Hu et al. 2011). Together, BRCA1, BARD1, UIMC1, FAM175A, BRCC36, BRE and BABAM1 form the so-called BRCA1-A complex at DNA DSBs (Wang et al. 2009).
Literature References
PubMed ID Title Journal Year
21282113 NBA1/MERIT40 and BRE interaction is required for the integrity of two distinct deubiquitinating enzyme BRCC36-containing complexes

Liu, J, Hu, X, Castillo, A, Kim, JA, Huang, M, Wang, B

J. Biol. Chem. 2011
24667604 Role of MERIT40 in stabilization of BRCA1 complex: a protein-protein interaction study

Varma, AK, Sawant, UU, Vikrant, -

Biochem. Biophys. Res. Commun. 2014
19261749 NBA1, a new player in the Brca1 A complex, is required for DNA damage resistance and checkpoint control

Hofmann, K, Hurov, K, Elledge, SJ, Wang, B

Genes Dev. 2009
17525340 Abraxas and RAP80 form a BRCA1 protein complex required for the DNA damage response

Elledge, SJ, Matsuoka, S, Gygi, SP, Wang, B, Smogorzewska, A, Zhang, D, Ballif, BA

Science 2007
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Orthologous Events
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Authored
Orlic-Milacic, M  (2015-05-12)
Reviewed
Borowiec, JA  (2015-06-12)
Created
Orlic-Milacic, M  (2015-03-13)
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