2008
NAC1, a POZ/BTB protein that functions as a corepressor
Korutla L, Wang P, Jackson T, Mackler S. NAC1, a POZ/BTB protein that functions as a corepressor. Neurochemistry International 2008, 54: 245-252. PMID: 19121354, DOI: 10.1016/j.neuint.2008.12.008.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCell LineCentral Nervous SystemGenes, ReporterHumansKruppel-Like Transcription FactorsMiceNeoplasm ProteinsNerve Tissue ProteinsPromyelocytic Leukemia Zinc Finger ProteinProtein IsoformsProtein Structure, TertiaryProto-Oncogene ProteinsRecombinant Fusion ProteinsRepressor ProteinsTranscription, GeneticConceptsPOZ/BTB proteinBTB proteinsPOZ/BTB domainFusion proteinVP16 activation domainGST pulldown assaysGAL4 fusion proteinsTranscriptional repressor proteinZinc finger proteinProtein-protein interactionsB fusion proteinFinger proteinActivation domainTransient assaysNAC1 functionPulldown assaysRepressor proteinBTB domainNon-neuronal cellsTranscriptional inhibitionCorepressorNeuronal cellsProteinMature CNSSelective interaction
2007
NAC1, a cocaine‐regulated POZ/BTB protein interacts with CoREST
Korutla L, Degnan R, Wang P, Mackler S. NAC1, a cocaine‐regulated POZ/BTB protein interacts with CoREST. Journal Of Neurochemistry 2007, 101: 611-618. PMID: 17254023, DOI: 10.1111/j.1471-4159.2006.04387.x.Peer-Reviewed Original ResearchConceptsPOZ/BTB proteinPOZ/BTB domainBTB proteinsBTB domainProtein-protein interactionsHEK293T cellsNeuro-2a cellsT cellsTranscriptional regulatorsRepressor proteinRat brain samplesBrain samplesCoRESTCoimmunoprecipitation studiesHomodimer formationHomodimer assemblyRepressor mechanismProtein expressionProteinDirect interactionEndogenous interactionPresent studyPox virus
2005
The POZ/BTB protein NAC1 interacts with two different histone deacetylases in neuronal‐like cultures
Korutla L, Wang P, Mackler S. The POZ/BTB protein NAC1 interacts with two different histone deacetylases in neuronal‐like cultures. Journal Of Neurochemistry 2005, 94: 786-793. PMID: 16033423, DOI: 10.1111/j.1471-4159.2005.03206.x.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAnimals, NewbornBlotting, WesternButyratesCells, CulturedEnzyme InhibitorsGene Expression RegulationHippocampusHistone DeacetylasesHumansHydroxamic AcidsImmunoprecipitationMiceNerve Tissue ProteinsNeuroblastomaNeuronsPlasmidsProtein BindingProtein IsoformsRatsRepressor ProteinsTranscription, GeneticTransfectionTwo-Hybrid System TechniquesConceptsPOZ/BTB proteinProtein-protein interactionsBTB proteinsHistone deacetylasesPOZ domainTwo-hybridGlutathione S-transferase pulldownRecruit histone deacetylasesDifferent histone deacetylasesTranscriptional repressionGST pulldownSNAC1Histone deacetylase inhibitionCorepressorDeacetylasesRepressionDeacetylase inhibitionProteinPulldownHDAC-3NaC1MSin3ANucleus accumbensCNS regionsCoimmunoprecipitation
2002
Differences in expression, actions and cocaine regulation of two isoforms for the brain transcriptional regulator NAC1
Korutla L, Wang P, Lewis D, Neustadter J, Stromberg M, Mackler S. Differences in expression, actions and cocaine regulation of two isoforms for the brain transcriptional regulator NAC1. Neuroscience 2002, 110: 421-429. PMID: 11906783, DOI: 10.1016/s0306-4522(01)00518-8.Peer-Reviewed Original ResearchConceptsBTB/POZ proteinPOZ proteinShort isoformDNA binding domainsPost-transcriptional processingSemi-quantitative reverse transcription-polymerase chain reaction analysisPeripheral tissuesRat brainTranscriptional repressionSubnuclear localizationTranscription-polymerase chain reaction analysisBinding domainsReverse transcription-polymerase chain reaction analysisReporter systemCell cycleCocaine-induced locomotionRat nucleus accumbensWestern blot analysisTranscriptionAmino acidsIsoformsProteinChain reaction analysisBlot analysisNeuronal function
2000
Activation of surfactant protein‐B transcription: Signaling through the SP‐A receptor utilizing the PI3 kinase pathway
Strayer D, Korutla L. Activation of surfactant protein‐B transcription: Signaling through the SP‐A receptor utilizing the PI3 kinase pathway. Journal Of Cellular Physiology 2000, 184: 229-238. PMID: 10867648, DOI: 10.1002/1097-4652(200008)184:2<229::aid-jcp11>3.0.co;2-x.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCells, CulturedDNA-Binding ProteinsFemaleGlycoproteinsHepatocyte Nuclear Factor 3-alphaLungNuclear ProteinsPhosphatidylinositol 3-KinasesPromoter Regions, GeneticProtein IsoformsProteolipidsPulmonary Surfactant-Associated Protein APulmonary Surfactant-Associated ProteinsPulmonary SurfactantsRatsReceptors, Cell SurfaceThyroid Nuclear Factor 1Transcription FactorsTranscription, GeneticConceptsSP-B promoterSP-B transcriptionPI3-kinaseHNF-3Consensus recognition elementSurfactant proteinsPI3-kinase pathwaySP-A receptorGel shift analysisCell transcriptional activityKinase localizationCellular functionsInteraction of SPTranscription factorsCell biologyNuclear localizationPlasma membraneKinase pathwayTranscriptional activityTranscriptionProteinSpCognate receptorsPromoterType II cells