Dephosphorylation of the C-terminal tyrosyl residue of the DNA damage-related histone H2A. X is mediated by the protein phosphatase eyes absent
N Krishnan, DG Jeong, SK Jung, SE Ryu, A Xiao… - Journal of Biological …, 2009 - jbc.org
In mammalian cells, the DNA damage-related histone H2A variant H2A. X is characterized
by a C-terminal tyrosyl residue, Tyr-142, which is phosphorylated by an atypical kinase,
WSTF. The phosphorylation status of Tyr-142 in H2A. X has been shown to be an important
regulator of the DNA damage response by controlling the formation of γH2A. X foci, which
are platforms for recruiting molecules involved in DNA damage repair and signaling. In this
work, we present evidence to support the identification of the Eyes Absent (EYA) …
by a C-terminal tyrosyl residue, Tyr-142, which is phosphorylated by an atypical kinase,
WSTF. The phosphorylation status of Tyr-142 in H2A. X has been shown to be an important
regulator of the DNA damage response by controlling the formation of γH2A. X foci, which
are platforms for recruiting molecules involved in DNA damage repair and signaling. In this
work, we present evidence to support the identification of the Eyes Absent (EYA) …
