2009
Dephosphorylation of the C-terminal Tyrosyl Residue of the DNA Damage-related Histone H2A.X Is Mediated by the Protein Phosphatase Eyes Absent*
Krishnan N, Jeong DG, Jung SK, Ryu SE, Xiao A, Allis CD, Kim SJ, Tonks NK. Dephosphorylation of the C-terminal Tyrosyl Residue of the DNA Damage-related Histone H2A.X Is Mediated by the Protein Phosphatase Eyes Absent*. Journal Of Biological Chemistry 2009, 284: 16066-16070. PMID: 19351884, PMCID: PMC2713548, DOI: 10.1074/jbc.c900032200.Peer-Reviewed Original ResearchMeSH KeywordsCell Line, TumorDNA DamageDNA-Binding ProteinsElectrochemistryHistonesHumansIntracellular Signaling Peptides and ProteinsMetalsNuclear ProteinsPhosphorylationProtein Structure, TertiaryProtein Tyrosine Phosphatase, Non-Receptor Type 1Protein Tyrosine PhosphatasesRNA InterferenceSubstrate SpecificityTransfectionTyrosineConceptsEyes AbsentDNA damage responseTyr-142Damage responseTyrosyl residuesProtein tyrosine phosphataseDNA damage repairAtypical kinaseHistone H2A.X.Haloacid dehalogenaseMammalian cellsHistone H2A.XDisplayed specificityElevated basal phosphorylationPhosphorylation statusRNA interferenceDamage repairPhysiological substratesH2A.XNovel roleBasal phosphorylationImportant regulatorDephosphorylationResiduesWSTFA distinct H2A.X isoform is enriched in Xenopus laevis eggs and early embryos and is phosphorylated in the absence of a checkpoint
Shechter D, Chitta RK, Xiao A, Shabanowitz J, Hunt DF, Allis CD. A distinct H2A.X isoform is enriched in Xenopus laevis eggs and early embryos and is phosphorylated in the absence of a checkpoint. Proceedings Of The National Academy Of Sciences Of The United States Of America 2009, 106: 749-754. PMID: 19131518, PMCID: PMC2630098, DOI: 10.1073/pnas.0812207106.Peer-Reviewed Original ResearchConceptsDNA damageEarly embryosSignificance of phosphorylationTerminal consensus sequenceExogenous DNA damageDNA damage responseCell-free egg extractsPhospho-specific antibodiesEarly cell cyclesFrog Xenopus laevisMulticellular organismsH2A variantsXenopus tropicalisDamage responseUnannotated isoformsMammalian cellsHistone H2A.XSomatic cellsCheckpoint conditionsXenopus laevis eggsAquatic speciesEgg extractsConsensus sequenceCell cycleH2A.X
2008
WSTF regulates the H2A.X DNA damage response via a novel tyrosine kinase activity
Xiao A, Li H, Shechter D, Ahn SH, Fabrizio LA, Erdjument-Bromage H, Ishibe-Murakami S, Wang B, Tempst P, Hofmann K, Patel DJ, Elledge SJ, Allis CD. WSTF regulates the H2A.X DNA damage response via a novel tyrosine kinase activity. Nature 2008, 457: 57-62. PMID: 19092802, PMCID: PMC2854499, DOI: 10.1038/nature07668.Peer-Reviewed Original ResearchConceptsDNA damage responseIntrinsic tyrosine kinase activityTyrosine kinase activityDamage responseKinase activityWilliams-Beuren syndrome transcription factorDouble-strand break responseNew regulatory mechanismWICH complexKinase foldEukaryotic cellsTranscription factorsWSTFKnowledge of domainsGenomic instabilityBreak responseSequence homologyRegulatory mechanismsCell deathPrecise rolePhosphorylationRepair processNew mechanismChromatinImportant role
2004
Linking the epigenetic ‘language’ of covalent histone modifications to cancer
Hake SB, Xiao A, Allis CD. Linking the epigenetic ‘language’ of covalent histone modifications to cancer. British Journal Of Cancer 2004, 90: 761-769. PMID: 14970850, PMCID: PMC2410168, DOI: 10.1038/sj.bjc.6601575.Peer-Reviewed Original ResearchConceptsCovalent histone modificationsHistone modificationsMethylation of DNAChromatin reorganisationEpigenetic modulationCovalent modificationHuman biologyHuman cancersMultistep processMethylationRecent findingsChromatinHuman healthHistonesEpigeneticsPhosphorylationBiologyAcetylationDNAModificationPotential therapyCarcinogenesisMajor partCancer