2023
Mammalian SWI/SNF chromatin remodeling complexes promote tyrosine kinase inhibitor resistance in EGFR-mutant lung cancer
de Miguel F, Gentile C, Feng W, Silva S, Sankar A, Exposito F, Cai W, Melnick M, Robles-Oteiza C, Hinkley M, Tsai J, Hartley A, Wei J, Wurtz A, Li F, Toki M, Rimm D, Homer R, Wilen C, Xiao A, Qi J, Yan Q, Nguyen D, Jänne P, Kadoch C, Politi K. Mammalian SWI/SNF chromatin remodeling complexes promote tyrosine kinase inhibitor resistance in EGFR-mutant lung cancer. Cancer Cell 2023, 41: 1516-1534.e9. PMID: 37541244, PMCID: PMC10957226, DOI: 10.1016/j.ccell.2023.07.005.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsChromatinChromatin Assembly and DisassemblyDNA HelicasesErbB ReceptorsHumansLung NeoplasmsMammalsMutationNuclear ProteinsProtein Kinase InhibitorsTranscription FactorsConceptsMammalian SWI/SNF chromatinSWI/SNF chromatinMSWI/SNF complexesGenome-wide localizationGene regulatory signaturesNon-genetic mechanismsEpithelial cell differentiationEGFR-mutant cellsChromatin accessibilitySNF complexCellular programsRegulatory signaturesTKI-resistant lung cancerGene targetsKinase inhibitor resistanceCell differentiationMesenchymal transitionTKI resistancePharmacologic disruptionTyrosine kinase inhibitor resistanceCell proliferationChromatinInhibitor resistanceEGFR-mutant lungKinase inhibitors
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 ResearchMeSH KeywordsAcetylationCell Transformation, NeoplasticChromatin Assembly and DisassemblyDNA MethylationGene Expression Regulation, NeoplasticHistonesHumansNeoplasmsPhosphorylationConceptsCovalent histone modificationsHistone modificationsMethylation of DNAChromatin reorganisationEpigenetic modulationCovalent modificationHuman biologyHuman cancersMultistep processMethylationRecent findingsChromatinHuman healthHistonesEpigeneticsPhosphorylationBiologyAcetylationDNAModificationPotential therapyCarcinogenesisMajor partCancer