2024
Identification of coilin interactors reveals coordinated control of Cajal body number and structure
Escayola D, Zhang C, Nischwitz E, Schärfen L, Dörner K, Straube K, Kutay U, Butter F, Neugebauer K. Identification of coilin interactors reveals coordinated control of Cajal body number and structure. Journal Of Cell Biology 2024, 224: e202305081. PMID: 39602297, PMCID: PMC11602656, DOI: 10.1083/jcb.202305081.Peer-Reviewed Original ResearchConceptsCajal bodiesSurvival motor neuron proteinCB assemblyModulating posttranslational modificationsRegulate RNA processingProtein interactorsProximity biotinylationRNA processingGenetic lociPosttranslational modificationsGene activationTranscription factorsFunctional screeningBiomolecular condensatesCoilinNeuronal proteinsCell nucleiProteinNuclear levelsNuclear positivityCB componentsCB numberBody numberAssemblyRibosome
2018
Dynamics and Function of Nuclear Bodies during Embryogenesis
Escayola D, Neugebauer K. Dynamics and Function of Nuclear Bodies during Embryogenesis. Biochemistry 2018, 57: 2462-2469. PMID: 29473743, DOI: 10.1021/acs.biochem.7b01262.Peer-Reviewed Original ResearchConceptsNuclear bodiesCajal bodiesRNA processingZygotic gene productsRNA-protein complexesEfficient RNA processingFunction of nucleoliNuclear body formationGene elementsVariety of organismsZygotic genomeZygotic transitionGenomic lociNascent RNAModel organismsNuclear stepsTranscriptional activationEarly embryosNuclear proteinsGene productsGene locusMembraneless organellesBody formationExcellent modelCell nuclei
2017
Special focus on the Cajal Body
Neugebauer KM. Special focus on the Cajal Body. RNA Biology 2017, 14: 669-670. PMID: 28486008, PMCID: PMC5519238, DOI: 10.1080/15476286.2017.1316928.Peer-Reviewed Original Research
2015
Coilin: The first 25 years
Machyna M, Neugebauer KM, Staněk D. Coilin: The first 25 years. RNA Biology 2015, 12: 590-596. PMID: 25970135, PMCID: PMC4615369, DOI: 10.1080/15476286.2015.1034923.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCoiled BodiesHistory, 20th CenturyHistory, 21st CenturyHumansNuclear ProteinsProtein Processing, Post-Translational
2014
The Coilin Interactome Identifies Hundreds of Small Noncoding RNAs that Traffic through Cajal Bodies
Machyna M, Kehr S, Straube K, Kappei D, Buchholz F, Butter F, Ule J, Hertel J, Stadler PF, Neugebauer KM. The Coilin Interactome Identifies Hundreds of Small Noncoding RNAs that Traffic through Cajal Bodies. Molecular Cell 2014, 56: 389-399. PMID: 25514182, DOI: 10.1016/j.molcel.2014.10.004.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCell CycleCell NucleolusCoiled BodiesHeLa CellsHumansMiceNuclear ProteinsProtein BindingRNA TransportRNA, Small UntranslatedConceptsCajal bodiesSmall nucleolar RNAsSmall nuclear RNASmall noncoding RNAsChIP-seq peaksCoilin proteinSnoRNA biogenesisRNP assemblySnRNP assemblyNcRNA metabolismSnRNA genesSubnuclear compartmentsCellular hubHuman snoRNAsMolecular functionsSnRNA transcriptsNucleolar RNAsNoncoding RNAsNuclear RNACoilinRNASignal trafficRole of CBAssemblySnRNAs
2010
Coilin-dependent snRNP assembly is essential for zebrafish embryogenesis
Strzelecka M, Trowitzsch S, Weber G, Lührmann R, Oates AC, Neugebauer KM. Coilin-dependent snRNP assembly is essential for zebrafish embryogenesis. Nature Structural & Molecular Biology 2010, 17: 403-409. PMID: 20357773, DOI: 10.1038/nsmb.1783.Peer-Reviewed Original ResearchDynamic control of Cajal body number during zebrafish embryogenesis
Strzelecka M, Oates AC, Neugebauer KM. Dynamic control of Cajal body number during zebrafish embryogenesis. Nucleus 2010, 1: 96-108. PMID: 21327108, PMCID: PMC3035118, DOI: 10.4161/nucl.1.1.10680.Peer-Reviewed Original ResearchConceptsCajal bodiesEnd processing factorsGene expressionZygotic genome activationZygotic gene expressionRNA processing machineryDistinct nuclear bodiesMRNA splicing machineryCajal body numberLive-cell imagingCB numberHours of developmentGenome activationZebrafish embryogenesisNuclear subcompartmentsSnRNP biogenesisSplicing machineryZebrafish embryosCell divisionNuclear bodiesCB assemblyEmbryonic cellsMaternal contributionProcessing machineryEmbryos
2009
SR Protein Family Members Display Diverse Activities in the Formation of Nascent and Mature mRNPs In Vivo
Sapra AK, Änkö M, Grishina I, Lorenz M, Pabis M, Poser I, Rollins J, Weiland EM, Neugebauer KM. SR Protein Family Members Display Diverse Activities in the Formation of Nascent and Mature mRNPs In Vivo. Molecular Cell 2009, 34: 179-190. PMID: 19394295, DOI: 10.1016/j.molcel.2009.02.031.Peer-Reviewed Original ResearchMeSH KeywordsChromatin ImmunoprecipitationChromosomes, Artificial, BacterialFluorescence Resonance Energy TransferGenes, fosGreen Fluorescent ProteinsHeLa CellsHumansNuclear ProteinsPromoter Regions, GeneticRecombinant Fusion ProteinsRibonucleoproteinsRNA SplicingRNA-Binding ProteinsTranscription, GeneticConceptsRNA recognition motifSR proteinsCytoplasmic mRNAPol IIProtein interactionsSR protein family membersFRET/FLIMMRNA splicing factorsProtein family membersStable cell linesMRNP remodelingMRNA lifetimeGene regulationFormation of nascentSplicing factorsRecognition motifPromoter controlFamily membersAdditional roleProteinRNACell linesIndividual family membersMRNADiverse activities
2000
SR proteins are autoantigens in patients with systemic lupus erythematosus: Importance of phosphoepitopes
Neugebauer K, Merrill J, Wener M, Lahita R, Roth M. SR proteins are autoantigens in patients with systemic lupus erythematosus: Importance of phosphoepitopes. Arthritis & Rheumatism 2000, 43: 1768-1778. PMID: 10943867, DOI: 10.1002/1529-0131(200008)43:8<1768::aid-anr13>3.0.co;2-9.Peer-Reviewed Original ResearchConceptsSystemic lupus erythematosusEnzyme-linked immunosorbent assaySLE patientsLupus erythematosusDiagnosis of SLEPrimary antiphospholipid syndromeGroup of patientsSera of patientsAntiphospholipid syndromeProtein reactivityRheumatoid arthritisPatient seraPatientsAutoantigensImmunosorbent assayAntigen recognitionSerumErythematosusFurther studiesSeparate groupsDisordersBind dsDNAArthritisAutoantibodiesAutoimmunity
1997
Distribution of pre-mRNA splicing factors at sites of RNA polymerase II transcription.
Neugebauer K, Roth M. Distribution of pre-mRNA splicing factors at sites of RNA polymerase II transcription. Genes & Development 1997, 11: 1148-1159. PMID: 9159396, DOI: 10.1101/gad.11.9.1148.Peer-Reviewed Original ResearchMeSH KeywordsAntibodies, MonoclonalBinding SitesCell NucleusFluorescent Antibody Technique, IndirectHeLa CellsHumansNuclear ProteinsPhosphoproteinsRibonucleoproteins, Small NuclearRNA Polymerase IIRNA PrecursorsRNA SplicingRNA-Binding ProteinsSerine-Arginine Splicing FactorsTranscription, GeneticUridine TriphosphateConceptsRNA polymerase II transcriptionPolymerase II transcriptionMRNA splicing factorsSplicing factorsSR familyPre-mRNA splicingVisualization of hundredsHeLa cell nucleiSplicing regulatorsActive genesTranscription unitMRNA splicingGene regulatorsGene transcriptionPre-mRNADistinct functionsRNA synthesisTranscriptionCell nucleiSplicingSingle memberRegulatorActive site
1995
A conserved epitope on a subset of SR proteins defines a larger family of Pre-mRNA splicing factors.
Neugebauer K, Stolk J, Roth M. A conserved epitope on a subset of SR proteins defines a larger family of Pre-mRNA splicing factors. Journal Of Cell Biology 1995, 129: 899-908. PMID: 7538140, PMCID: PMC2120486, DOI: 10.1083/jcb.129.4.899.Peer-Reviewed Original Research