EYA1-4 dephosphorylates tyrosine Y142 of H2AFX

Stable Identifier
Reaction [transition]
Homo sapiens
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In response to DNA damage, EYA tyrosine protein phosphatases (EYA1, EYA2, EYA3 and, by sequence similarity, EYA4) dephosphorylate tyrosine Y142 of H2AFX, which allows the progression of DNA repair (Cook et al. 2009, Krishnan et al. 2009). It is possible that different EYA proteins heterodimerize in different cell types - the existence of a functional EYA1:EYA3 heterodimer in human embryonic kidney 293 (HEK293) cells is likely (Cook et al. 2009).

MCPH1 recognizes and binds diphosphorylated H2AFX, but the exact biological role of this interaction has not been elucidated (Singh et al. 2012).

Literature References
PubMed ID Title Journal Year
22908299 Dual recognition of phosphoserine and phosphotyrosine in histone variant H2A.X by DNA damage response protein MCPH1

Singh, N, Mer, G, Wiltshire, TD, Héroux, A, Basnet, H, Couch, FJ, Thompson, JR, Rosenfeld, MG, Mohammad, DH, Botuyan, MV, Yaffe, MB

Proc. Natl. Acad. Sci. U.S.A. 2012
19351884 Dephosphorylation of the C-terminal tyrosyl residue of the DNA damage-related histone H2A.X is mediated by the protein phosphatase eyes absent

Ryu, SE, Kim, SJ, Krishnan, N, Tonks, NK, Jeong, DG, Jung, SK, Xiao, A, Allis, CD

J. Biol. Chem. 2009
19234442 Tyrosine dephosphorylation of H2AX modulates apoptosis and survival decisions

Telese, F, Wang, X, Cook, PJ, Rosenfeld, MG, Glass, CK, Ju, BG

Nature 2009
Catalyst Activity

protein tyrosine phosphatase activity of p-EYA1-4 [nucleoplasm]

Orthologous Events
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