2013
Higher-Order Looping and Nuclear Organization of Tcra Facilitate Targeted RAG Cleavage and Regulated Rearrangement in Recombination Centers
Chaumeil J, Micsinai M, Ntziachristos P, Deriano L, Wang J, Ji Y, Nora EP, Rodesch MJ, Jeddeloh JA, Aifantis I, Kluger Y, Schatz DG, Skok JA. Higher-Order Looping and Nuclear Organization of Tcra Facilitate Targeted RAG Cleavage and Regulated Rearrangement in Recombination Centers. Cell Reports 2013, 3: 359-370. PMID: 23416051, PMCID: PMC3664546, DOI: 10.1016/j.celrep.2013.01.024.Peer-Reviewed Original ResearchMeSH KeywordsAllelesAnimalsAtaxia Telangiectasia Mutated ProteinsCell Cycle ProteinsCell NucleusDNA DamageDNA-Binding ProteinsGenetic LociGenomic InstabilityHistonesHomeodomain ProteinsMiceMice, Inbred C57BLMice, Inbred CBAMice, KnockoutProtein Serine-Threonine KinasesReceptors, Antigen, T-Cell, alpha-betaTumor Suppressor ProteinsV(D)J RecombinationConceptsAntigen receptor lociRegulated rearrangementsGenome stabilityNuclear organizationRAG cleavageRAG recombinaseNuclear accessibilityRAG bindingCellular transformationΑ locusRecombination eventsReceptor locusDiverse arrayCell receptorLociLoop formationTight controlRegulationCleavageFocal bindingGenetic anomaliesBindingKey determinantRearrangementTranscriptionThe Ataxia Telangiectasia mutated kinase controls Igκ allelic exclusion by inhibiting secondary Vκ-to-Jκ rearrangements
Steinel NC, Lee BS, Tubbs AT, Bednarski JJ, Schulte E, Yang-Iott KS, Schatz DG, Sleckman BP, Bassing CH. The Ataxia Telangiectasia mutated kinase controls Igκ allelic exclusion by inhibiting secondary Vκ-to-Jκ rearrangements. Journal Of Experimental Medicine 2013, 210: 233-239. PMID: 23382544, PMCID: PMC3570110, DOI: 10.1084/jem.20121605.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAllelesAnimalsAtaxia Telangiectasia Mutated ProteinsBase SequenceB-LymphocytesCell Cycle ProteinsDNA Breaks, Double-StrandedDNA-Binding ProteinsGene Rearrangement, B-Lymphocyte, Light ChainHistonesHomeodomain ProteinsImmunoglobulin kappa-ChainsIntracellular Signaling Peptides and ProteinsMiceMice, 129 StrainMice, KnockoutModels, BiologicalProtein Serine-Threonine KinasesRNA, MessengerSignal TransductionTumor Suppressor ProteinsConceptsDNA double-strand breaksRAG DNA double-strand breaksAllelic exclusionIgκ rearrangementAtaxia telangiectasiaProtein kinase kinaseAntigen receptor chainsDouble-strand breaksHistone H2AX phosphorylationFeedback inhibitionATM kinaseIgκ recombinationKinase kinaseDNA-PKConcomitant repressionH2AX phosphorylationRAG endonucleaseReceptor chainsMDC1H2AXKinaseAllelesRecombinationRearrangementTelangiectasia
2012
A Dual Interaction between the DNA Damage Response Protein MDC1 and the RAG1 Subunit of the V(D)J Recombinase*
Coster G, Gold A, Chen D, Schatz DG, Goldberg M. A Dual Interaction between the DNA Damage Response Protein MDC1 and the RAG1 Subunit of the V(D)J Recombinase*. Journal Of Biological Chemistry 2012, 287: 36488-36498. PMID: 22942284, PMCID: PMC3476314, DOI: 10.1074/jbc.m112.402487.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAmino Acid MotifsBRCA1 ProteinCell Cycle ProteinsCell Line, TumorHistonesHomeodomain ProteinsHumansModels, BiologicalNuclear ProteinsPeptide MappingPhosphorylationProtein Structure, TertiaryRepetitive Sequences, Amino AcidTrans-ActivatorsVDJ RecombinasesConceptsDNA double-strand breaksDNA damage responseTandem BRCA1 C-terminal (BRCT) domainsC-terminusSpecific DNA double-strand breaksBRCA1 C-terminal domainC-terminal domainThreonine-rich repeatsDouble-strand breaksRAG1 subunitRAG recombinaseRAG2 proteinsDDR proteinsDamage responseRegulatory signalsBinding interfaceBreak siteHistone H2AXRAG activityRich repeatsNon-core regionsMDC1RAG1PhosphorylationSubsequent signal amplification
2011
A role for cohesin in T-cell-receptor rearrangement and thymocyte differentiation
Seitan VC, Hao B, Tachibana-Konwalski K, Lavagnolli T, Mira-Bontenbal H, Brown KE, Teng G, Carroll T, Terry A, Horan K, Marks H, Adams DJ, Schatz DG, Aragon L, Fisher AG, Krangel MS, Nasmyth K, Merkenschlager M. A role for cohesin in T-cell-receptor rearrangement and thymocyte differentiation. Nature 2011, 476: 467-471. PMID: 21832993, PMCID: PMC3179485, DOI: 10.1038/nature10312.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCell Cycle ProteinsCell DifferentiationChromosomal Proteins, Non-HistoneDNA-Binding ProteinsGene Expression RegulationGene Rearrangement, T-LymphocyteGenes, RAG-1MiceNuclear ProteinsPhosphoproteinsReceptors, Antigen, T-Cell, alpha-betaRecombinasesThymus GlandTranscription, Genetic
2009
RAG-1 and ATM coordinate monoallelic recombination and nuclear positioning of immunoglobulin loci
Hewitt SL, Yin B, Ji Y, Chaumeil J, Marszalek K, Tenthorey J, Salvagiotto G, Steinel N, Ramsey LB, Ghysdael J, Farrar MA, Sleckman BP, Schatz DG, Busslinger M, Bassing CH, Skok JA. RAG-1 and ATM coordinate monoallelic recombination and nuclear positioning of immunoglobulin loci. Nature Immunology 2009, 10: 655-664. PMID: 19448632, PMCID: PMC2693356, DOI: 10.1038/ni.1735.Peer-Reviewed Original ResearchAllelesAnimalsAtaxia Telangiectasia Mutated ProteinsB-LymphocytesCell Cycle ProteinsCells, CulturedDNA BreaksDNA-Binding ProteinsGene RearrangementHomeodomain ProteinsImmunoglobulinsMiceMice, Inbred C57BLMice, KnockoutProtein Serine-Threonine KinasesRecombination, GeneticTumor Suppressor ProteinsVDJ Recombinases