2018
Striatin-1 is a B subunit of protein phosphatase PP2A that regulates dendritic arborization and spine development in striatal neurons
Li D, Musante V, Zhou W, Picciotto MR, Nairn AC. Striatin-1 is a B subunit of protein phosphatase PP2A that regulates dendritic arborization and spine development in striatal neurons. Journal Of Biological Chemistry 2018, 293: 11179-11194. PMID: 29802198, PMCID: PMC6052221, DOI: 10.1074/jbc.ra117.001519.Peer-Reviewed Original ResearchConceptsSerine/threonine phosphatase PP2AStriatin-interacting phosphataseRNA knockdown approachB subunitSTRIPAK complexPhosphatase PP2AProtein phosphataseMultiprotein complexesKnockdown approachStriatin familyMutant constructsStriatal neuronal culturesPP2ANeuronal developmentPrimary striatal neuronal culturesDendritic phenotypeKnockdown modelSynapse formationSubunitsSpine developmentSelective roleReduced expressionNeuron maturationNeuronal culturesStriatal neurons
2017
Reciprocal regulation of ARPP-16 by PKA and MAST3 kinases provides a cAMP-regulated switch in protein phosphatase 2A inhibition
Musante V, Li L, Kanyo J, Lam TT, Colangelo CM, Cheng SK, Brody AH, Greengard P, Le Novère N, Nairn AC. Reciprocal regulation of ARPP-16 by PKA and MAST3 kinases provides a cAMP-regulated switch in protein phosphatase 2A inhibition. ELife 2017, 6: e24998. PMID: 28613156, PMCID: PMC5515580, DOI: 10.7554/elife.24998.Peer-Reviewed Original ResearchConceptsARPP-16ARPP-19Protein phosphatase 2A inhibitionProtein phosphatase PP2A.Inhibition of PP2ASwitch-like responseKinase inhibitsPhosphatase PP2A.Regulatory interactionsPKA phosphorylationAntagonistic interplayReciprocal regulationBasal phosphorylationPhosphorylationMAST3PP2APKAENSAKinaseStriatal signalingPP2A.Multiple sitesInhibitionMitosisSignalingARPP-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 ResearchConceptsSerine/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
2011
Beyond the Dopamine Receptor: Regulation and Roles of Serine/Threonine Protein Phosphatases
Walaas SI, Hemmings HC, Greengard P, Nairn AC. Beyond the Dopamine Receptor: Regulation and Roles of Serine/Threonine Protein Phosphatases. Frontiers In Neuroanatomy 2011, 5: 50. PMID: 21904525, PMCID: PMC3162284, DOI: 10.3389/fnana.2011.00050.Peer-Reviewed Original ResearchSerine/threonine proteinARPP-16Signaling pathwaysDARPP-32Striatal signaling pathwaysRegulator of calmodulinMultiple neurological diseasesNovel roleMolecular actionsProteinPP1Monophosphate-regulated phosphoproteinPhosphoproteinMolecular integratorPleiotropic actionsMultiple stepsMajor subclassesDopamine receptorsPathwayHuntington's diseaseRecent studiesStriatal signalingPP2ACentral nervous systemPP2B
2001
Mechanisms for Increased Levels of Phosphorylation of Elongation Factor-2 during Hibernation in Ground Squirrels †
Chen Y, Matsushita M, Nairn A, Damuni Z, Cai D, Frerichs K, Hallenbeck J. Mechanisms for Increased Levels of Phosphorylation of Elongation Factor-2 during Hibernation in Ground Squirrels †. Biochemistry 2001, 40: 11565-11570. PMID: 11560506, DOI: 10.1021/bi010649w.Peer-Reviewed Original ResearchConceptsEukaryotic elongation factor 2EEF-2 phosphorylationElongation factor 2Elongation phaseEEF-2 kinase activityProtein phosphatase 2AGround squirrelsLevel of phosphorylationFactor 2Phosphatase 2ACellular functionsCatalytic subunitUncharacterized mechanismKinase activityInhibitor 2Protein synthesisPhosphorylationPP2AHibernating animalsActive animalsHibernatorsReversible mechanismSevere reductionSquirrelsHibernation
1997
A molecular modeling analysis of the binding interactions between the okadaic acid class of natural product inhibitors and the ser-thr phosphatases, PP1 and PP2A
Gauss C, Sheppeck J, Nairn A, Chamberlin R. A molecular modeling analysis of the binding interactions between the okadaic acid class of natural product inhibitors and the ser-thr phosphatases, PP1 and PP2A. Bioorganic & Medicinal Chemistry 1997, 5: 1751-1773. PMID: 9354231, DOI: 10.1016/s0968-0896(97)00145-4.Peer-Reviewed Original ResearchConceptsSerine-threonine proteinOkadaic acid classSignal transduction pathwaysNatural product inhibitorsCatalytic subunitTransduction pathwaysPP1Endogenous substratesProduct inhibitorsMolecular modeling analysisSer-ThrAcid classPP2AImportant roleComputer-generated modelsInhibitorsSubunitsProteinPathway