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 ResearchConceptsMammalian 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
2014
The Developmental Potential of iPSCs Is Greatly Influenced by Reprogramming Factor Selection
Buganim Y, Markoulaki S, van Wietmarschen N, Hoke H, Wu T, Ganz K, Akhtar-Zaidi B, He Y, Abraham BJ, Porubsky D, Kulenkampff E, Faddah DA, Shi L, Gao Q, Sarkar S, Cohen M, Goldmann J, Nery JR, Schultz MD, Ecker JR, Xiao A, Young RA, Lansdorp PM, Jaenisch R. The Developmental Potential of iPSCs Is Greatly Influenced by Reprogramming Factor Selection. Cell Stem Cell 2014, 15: 295-309. PMID: 25192464, PMCID: PMC4170792, DOI: 10.1016/j.stem.2014.07.003.Peer-Reviewed Original ResearchAnimalsCell LineCellular ReprogrammingChimeraChromosomes, Human, Pair 8DNA MethylationEmbryonic Stem CellsEnhancer Elements, GeneticGene Expression ProfilingGenomeHistonesHumansInduced Pluripotent Stem CellsKruppel-Like Factor 4Mice, Inbred C57BLMice, Inbred DBARNA, MessengerTranscription FactorsTrisomyRif1 Maintains Telomere Length Homeostasis of ESCs by Mediating Heterochromatin Silencing
Dan J, Liu Y, Liu N, Chiourea M, Okuka M, Wu T, Ye X, Mou C, Wang L, Wang L, Yin Y, Yuan J, Zuo B, Wang F, Li Z, Pan X, Yin Z, Chen L, Keefe DL, Gagos S, Xiao A, Liu L. Rif1 Maintains Telomere Length Homeostasis of ESCs by Mediating Heterochromatin Silencing. Developmental Cell 2014, 29: 7-19. PMID: 24735877, PMCID: PMC4720134, DOI: 10.1016/j.devcel.2014.03.004.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsEmbryonic Stem CellsGene DeletionGene Expression Regulation, DevelopmentalGene SilencingHeterochromatinHistonesMethylationMiceProtein BindingProtein Processing, Post-TranslationalRecombination, GeneticRNA, MessengerTelomereTelomere HomeostasisTelomere-Binding ProteinsTranscription FactorsConceptsTelomere length homeostasisEmbryonic stem cellsLength homeostasisZscan4 expressionHeterochromatic silencingHeterochromatin silencingMethylation complexChromosomal fusionsEmbryonic lethalityGenomic stabilityTelomere elongationH3K9me3 levelsSubtelomeric regionsRecombination defectsLength heterogeneityStem cellsRIF1HomeostasisSilencingExpressionZscan4HyperrecombinationShRNALethalityInteracts
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 roleMethylation of RUNX1 by PRMT1 abrogates SIN3A binding and potentiates its transcriptional activity
Zhao X, Jankovic V, Gural A, Huang G, Pardanani A, Menendez S, Zhang J, Dunne R, Xiao A, Erdjument-Bromage H, Allis CD, Tempst P, Nimer SD. Methylation of RUNX1 by PRMT1 abrogates SIN3A binding and potentiates its transcriptional activity. Genes & Development 2008, 22: 640-653. PMID: 18316480, PMCID: PMC2259033, DOI: 10.1101/gad.1632608.Peer-Reviewed Original ResearchMeSH KeywordsAntigens, CD34ArginineCell Line, TumorCore Binding Factor Alpha 2 SubunitDNA-Binding ProteinsGene Expression RegulationHematopoiesisHumansMethylationMutationPlatelet Membrane Glycoprotein IIbProtein-Arginine N-MethyltransferasesProto-Oncogene ProteinsRepressor ProteinsRNA, Small InterferingRUNX1 Translocation Partner 1 ProteinSin3 Histone Deacetylase and Corepressor ComplexTrans-ActivatorsTranscription FactorsTranscription, GeneticConceptsRUNX1 functionArginine residuesRUNX1-ETO fusion proteinArginine methyltransferase PRMT1Arginine methylation sitesPRMT1-dependent methylationRUNX1 target genesProtein-protein interactionsPost-translational modificationsRUNX1/AML1Dominant inhibitory activityDefinitive hematopoiesisMethyltransferase PRMT1Corepressor Sin3ATranscriptional coactivatorPRMT1Target genesMethylation sitesDynamic regulationTranscriptional activityCorepressor bindingHuman acute leukemiaFusion proteinChromosome translocationRUNX1