2024
TRF2–RAP1 represses RAD51-dependent homology-directed telomere repair by promoting BLM-mediated D-loop unwinding and inhibiting BLM–DNA2-dependent 5′-end resection
Liang F, Rai R, Sodeinde T, Chang S. TRF2–RAP1 represses RAD51-dependent homology-directed telomere repair by promoting BLM-mediated D-loop unwinding and inhibiting BLM–DNA2-dependent 5′-end resection. Nucleic Acids Research 2024, 52: 9695-9709. PMID: 39082275, PMCID: PMC11381343, DOI: 10.1093/nar/gkae642.Peer-Reviewed Original ResearchHomology-directed repairTelomeric D-loopsD-loopChromosome fusionsD-loop formationSingle-stranded telomeric overhangsHomology searchTelomere clusteringTRFH domainPurified proteinBasic domainBlm mutantsProtect telomeresGenomic instabilityTelomeric overhangEnd resectionTRF2Molecular mechanismsTelomereTelomere lossMolecular pathwaysTelomere repairGenomeMutantsRap1
2023
Telomeres cooperate with the nuclear envelope to maintain genome stability
Rai R, Sodeinde T, Boston A, Chang S. Telomeres cooperate with the nuclear envelope to maintain genome stability. BioEssays 2023, 46: e2300184. PMID: 38047499, DOI: 10.1002/bies.202300184.Peer-Reviewed Original ResearchNuclear envelopeGenome stabilityNuclear envelope ruptureKu70/Ku80Homology-directed recombinationMammalian telomeresChromosome stabilityNuclear laminsShelterin componentsProtein TRF2Envelope ruptureRepair proteinsTelomeresRap1Recent findingsProteinFunction resultsRecombinationDNA sensingForm structuresLaminsTRF2Ku80DNAHomeostasisHomology directed telomere clustering, ultrabright telomere formation and nuclear envelope rupture in cells lacking TRF2B and RAP1
Rai R, Biju K, Sun W, Sodeinde T, Al-Hiyasat A, Morgan J, Ye X, Li X, Chen Y, Chang S. Homology directed telomere clustering, ultrabright telomere formation and nuclear envelope rupture in cells lacking TRF2B and RAP1. Nature Communications 2023, 14: 2144. PMID: 37059728, PMCID: PMC10104862, DOI: 10.1038/s41467-023-37761-w.Peer-Reviewed Original ResearchConceptsDouble-strand breaksNuclear envelopeDistinct DNA repair mechanismsNuclear envelope ruptureKu70/Ku80DNA repair mechanismsDNA-RNA hybridsBRCT domainGenome stabilityPhosphomimetic mutantTelomere formationGenotoxic stressEnvelope ruptureDysfunctional telomeresBasic domainRap1Aberrant laminTelomeresRepair mechanismsLaminsTRF2HomologyProteinShelterinADAR1p110
2011
A conserved motif within RAP1 has diversified roles in telomere protection and regulation in different organisms
Chen Y, Rai R, Zhou ZR, Kanoh J, Ribeyre C, Yang Y, Zheng H, Damay P, Wang F, Tsujii H, Hiraoka Y, Shore D, Hu HY, Chang S, Lei M. A conserved motif within RAP1 has diversified roles in telomere protection and regulation in different organisms. Nature Structural & Molecular Biology 2011, 18: 213-221. PMID: 21217703, PMCID: PMC3688267, DOI: 10.1038/nsmb.1974.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid MotifsAmino Acid SequenceAnimalsCells, CulturedCrystallography, X-RayFungal ProteinsHeLa CellsHumansModels, MolecularMolecular Sequence DataMutationNuclear Magnetic Resonance, BiomolecularProtein BindingProtein Interaction Domains and MotifsSaccharomycetalesSchizosaccharomycesShelterin ComplexTelomereTelomere-Binding ProteinsTelomeric Repeat Binding Protein 2ConceptsRap1 C-terminusDifferent interacting partnersProtein Rap1Fission yeastTelomere protectionInteracting partnerTranscriptional silencingDifferent organismsC-terminusFunctional analysisInteraction moduleYeastRap1Different functionsOrganismsTaz1Sir3TRF2MammalianTelomeresSilencingMammalsMotifCrystal structureRegulation