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Title 

Dephosphorylation of the C-terminal tyrosyl residue of the DNA damage-related histone H2A.X is mediated by the protein phosphatase eyes absent

 

Eya단백질에 의해 조절되는 DNA damage-related histone H2A.X의 C-terminal tyrosyl residue의 탈인산화

Authors 

N KrishnanDae Gwin JeongSuk Kyeong JungS E RyuA XiaoC D AllisSeung Jun KimN K Tonks

Publisher 

American Society for Biochemistry and Molecular Biology

Issue Date 

2009

Citation 

Journal of Biological Chemistry, vol. 284, no. 24, pp. 16066-16077

Abstract 

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?H2A.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) phosphatases, protein-tyrosine phosphatases of the haloacid dehalogenase superfamily, as being responsible for dephosphorylating the C-terminal tyrosyl residue of histone H2A.X. We demonstrate that EYA2 and EYA3 displayed specificity for Tyr-142 of H2A.X in assays in vitro. Suppression of eya3 by RNA interference resulted in elevated basal phosphorylation and inhibited DNA damage-induced dephosphorylation of Tyr-142 of H2A.X in vivo. This study provides the first indication of a physiological substrate for the EYA phosphatases and suggests a novel role for these enzymes in regulation of the DNA damage response.

ISSN 

0021-9258

Link 

http://dx.doi.org/10.1074/jbc.C900032200

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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