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

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dc.contributor.authorN Krishnan-
dc.contributor.authorDae Gwin Jeong-
dc.contributor.authorSuk Kyeong Jung-
dc.contributor.authorS E Ryu-
dc.contributor.authorA Xiao-
dc.contributor.authorC D Allis-
dc.contributor.authorSeung Jun Kim-
dc.contributor.authorN K Tonks-
dc.date.accessioned2017-04-19T09:13:59Z-
dc.date.available2017-04-19T09:13:59Z-
dc.date.issued2009-
dc.identifier.issn0021-9258-
dc.identifier.uri10.1074/jbc.C900032200ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/8990-
dc.description.abstractIn 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.-
dc.publisherAmer Soc Biochemistry Molecular Biology Inc-
dc.titleDephosphorylation 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-
dc.title.alternativeDephosphorylation of the C-terminal tyrosyl residue of the DNA damage-related histone H2A.X is mediated by the protein phosphatase eyes absent-
dc.typeArticle-
dc.citation.titleJournal of Biological Chemistry-
dc.citation.number24-
dc.citation.endPage16077-
dc.citation.startPage16066-
dc.citation.volume284-
dc.contributor.affiliatedAuthorDae Gwin Jeong-
dc.contributor.affiliatedAuthorSuk Kyeong Jung-
dc.contributor.affiliatedAuthorSeung Jun Kim-
dc.contributor.alternativeNameKrishnan-
dc.contributor.alternativeName정대균-
dc.contributor.alternativeName정숙경-
dc.contributor.alternativeName류성언-
dc.contributor.alternativeNameXiao-
dc.contributor.alternativeNameAllis-
dc.contributor.alternativeName김승준-
dc.contributor.alternativeNameTonks-
dc.identifier.bibliographicCitationJournal of Biological Chemistry, vol. 284, no. 24, pp. 16066-16077-
dc.identifier.doi10.1074/jbc.C900032200-
dc.description.journalClassY-
Appears in Collections:
Division of Research on National Challenges > Bionanotechnology Research Center > 1. Journal Articles
Critical Diseases Diagnostics Convergence Research Center > 1. Journal Articles
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