2017
ARPP-16 Is a Striatal-Enriched Inhibitor of Protein Phosphatase 2A Regulated by Microtubule-Associated Serine/Threonine Kinase 3 (Mast 3 Kinase)
Andrade EC, Musante V, Horiuchi A, Matsuzaki H, Brody AH, Wu T, Greengard P, Taylor JR, Nairn AC. ARPP-16 Is a Striatal-Enriched Inhibitor of Protein Phosphatase 2A Regulated by Microtubule-Associated Serine/Threonine Kinase 3 (Mast 3 Kinase). Journal Of Neuroscience 2017, 37: 2709-2722. PMID: 28167675, PMCID: PMC5354324, DOI: 10.1523/jneurosci.4559-15.2017.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCells, CulturedCorpus StriatumGene Expression Regulation, EnzymologicMaleMiceMice, Inbred C57BLMicrotubule-Associated ProteinsNeuronsPhosphoproteinsPhosphorylationProtein Phosphatase 2Protein Serine-Threonine KinasesConceptsSerine/threonine protein phosphataseSerine/threonine kinase 3Threonine protein phosphataseARPP-16Protein phosphataseKinase 3Protein phosphatase 2AProtein kinase A (PKA) signalingSmall acid-soluble proteinsKinase A SignalingAcid-soluble proteinsActivation of PKAPP2A substratesPhosphatase 2AARPP-16/19Heterotrimeric formMarked dephosphorylationSignal transductionSelective inhibitorPP2AA SignalingUnknown functionStriatal medium spiny neuronsMedium spiny neuronsSer46
2015
STEP61 is a substrate of the E3 ligase parkin and is upregulated in Parkinson’s disease
Kurup PK, Xu J, Videira RA, Ononenyi C, Baltazar G, Lombroso PJ, Nairn AC. STEP61 is a substrate of the E3 ligase parkin and is upregulated in Parkinson’s disease. Proceedings Of The National Academy Of Sciences Of The United States Of America 2015, 112: 1202-1207. PMID: 25583483, PMCID: PMC4313846, DOI: 10.1073/pnas.1417423112.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCorpus StriatumCyclic AMP Response Element-Binding ProteinDown-RegulationGene Expression Regulation, EnzymologicHEK293 CellsHumansMAP Kinase Signaling SystemMiceMice, KnockoutMitogen-Activated Protein Kinase 3MPTP PoisoningProtein Tyrosine Phosphatases, Non-ReceptorRatsRats, Sprague-DawleyUbiquitinationUbiquitin-Protein LigasesUp-RegulationConceptsE3 ubiquitin ligase ParkinSubstantia nigra pars compactaPathophysiology of PDProtein tyrosine phosphataseUbiquitin ligase ParkinSporadic Parkinson's diseaseE3 ligase ParkinRegulation of ParkinParkinson's diseaseTyrosine phosphataseParkin mutantsE3 ligaseProteasome systemDopaminergic neuronsDownstream targetsAutosomal recessive juvenile parkinsonismNovel substrateSTEP61ParkinCellular modelSTEP61 levelsSNc dopaminergic neuronsProtein levelsFunction contributesERK1/2
2001
Effects of chronic exposure to cocaine are regulated by the neuronal protein Cdk5
Bibb J, Chen J, Taylor J, Svenningsson P, Nishi A, Snyder G, Yan Z, Sagawa Z, Ouimet C, Nairn A, Nestler E, Greengard P. Effects of chronic exposure to cocaine are regulated by the neuronal protein Cdk5. Nature 2001, 410: 376-380. PMID: 11268215, DOI: 10.1038/35066591.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBrainCocaineCocaine-Related DisordersCorpus StriatumCyclin-Dependent Kinase 5Cyclin-Dependent KinasesDopamineDopamine and cAMP-Regulated Phosphoprotein 32Enzyme InhibitorsGene Expression Regulation, EnzymologicKinetinMaleMiceMice, TransgenicNerve Tissue ProteinsNeuronsOligonucleotide Array Sequence AnalysisPhosphoproteinsPhosphorylationProto-Oncogene Proteins c-fosPsychomotor PerformancePurinesRatsRats, Sprague-DawleyReceptors, Dopamine D1RoscovitineSignal TransductionConceptsTranscription factorsSuch transcription factorsDownstream target genesCyclin-dependent kinase 5DNA array analysisTarget genesGene expressionCocaine administrationKinase 5Inducible transgenic miceChronic exposureCdk5 inhibitorMessenger RNACocaine addictionArray analysisDopamine-mediated neurotransmissionDopamine-containing nerve terminalsMedium spiny neuronsD1 dopamine receptorsChronic cocaine administrationOverexpression of ΔFosBProteinTransgenic miceAdaptive changesSpiny neurons
2000
Regulation of protein phosphatase-1
Aggen J, Nairn A, Chamberlin R. Regulation of protein phosphatase-1. Cell Chemical Biology 2000, 7: r13-r23. PMID: 10662690, DOI: 10.1016/s1074-5521(00)00069-7.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsGene Expression Regulation, EnzymologicHumansMolecular Sequence DataPhosphoprotein PhosphatasesProtein Phosphatase 1Regulatory Sequences, Nucleic Acid
1996
Developmental expression of MARCKS and protein kinase C in mice in relation to the exencephaly resulting from MARCKS deficiency
Blackshear P, Lai W, Tuttle J, Stumpo D, Kennington E, Nairn A, Sulik K. Developmental expression of MARCKS and protein kinase C in mice in relation to the exencephaly resulting from MARCKS deficiency. Brain Research 1996, 96: 62-75. PMID: 8922669, DOI: 10.1016/0165-3806(96)00097-1.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBeta-GalactosidaseEmbryonic and Fetal DevelopmentGene Expression Regulation, DevelopmentalGene Expression Regulation, EnzymologicImmunohistochemistryIntracellular Signaling Peptides and ProteinsIsoenzymesMembrane ProteinsMiceMice, Inbred C57BLMice, TransgenicMyristoylated Alanine-Rich C Kinase SubstrateNerve Tissue ProteinsNeural Tube DefectsPhosphorylationProtein Kinase CProteinsRecombinant Fusion ProteinsConceptsProtein kinase CNeural tube closureKinase CPlasma membraneTube closureNeural tubeCranial neural tube closureMajor cellular substrateEmbryonic day 8.5MARCKS deficiencySpecific cell typesE8.5 embryosCranial neural tubeMouse geneFunctional defectsMARCKS proteinPerinatal lethalityMARCKSCellular substratesCranial neurulationMARCKS expressionUnderlying mesenchymeDevelopmental expressionPKC-alphaDay 8.5