2008
DARPP-32 Mediates the Actions of Multiple Drugs of Abuse
Svenningsson P, Nairn A, Greengard P. DARPP-32 Mediates the Actions of Multiple Drugs of Abuse. 2008, 3-16. DOI: 10.1007/978-0-387-76678-2_1.Peer-Reviewed Original ResearchPhosphorylation stateSerine/threonine protein phosphatasePP-1DARPP-32Threonine protein phosphataseState of phosphorylationProtein kinase A.Protein kinase AProtein phosphatasePhosphorylation sitesVirtue of regulationKinase AKey rolePhosphorylationThr34Potent inhibitorAdditional neurotransmittersCK2Ser97Behavioral responsesPhosphoproteinInhibitorsCK1Thr75Protein
1999
Protein phosphatase 1 modulation of neostriatal AMPA channels: regulation by DARPP–32 and spinophilin
Yan Z, Hsieh–Wilson L, Feng J, Tomizawa K, Allen P, Fienberg A, Nairn A, Greengard P. Protein phosphatase 1 modulation of neostriatal AMPA channels: regulation by DARPP–32 and spinophilin. Nature Neuroscience 1999, 2: 13-17. PMID: 10195174, DOI: 10.1038/4516.Peer-Reviewed Original ResearchConceptsPP-1Protein phosphatase 1DARPP-32Distinct molecular mechanismsPhosphatase 1Molecular mechanismsAMPA receptor-mediated synaptic transmissionPostsynaptic densityAMPA channelsRegulationSynaptic plasticitySpinophilinNeostriatal neuronsPlasticityPhysiological evidenceGlutamate channelsSynaptic transmissionAMPA receptorsPhosphoproteinProteinMechanismBindingActivityModulationCatalytic activity
1997
Site-directed mutagenesis of amino acid residues of protein phosphatase 1 involved in catalysis and inhibitor binding
Huang H, Horiuchi A, Goldberg J, Greengard P, Nairn A. Site-directed mutagenesis of amino acid residues of protein phosphatase 1 involved in catalysis and inhibitor binding. Proceedings Of The National Academy Of Sciences Of The United States Of America 1997, 94: 3530-3535. PMID: 9108010, PMCID: PMC20473, DOI: 10.1073/pnas.94.8.3530.Peer-Reviewed Original ResearchConceptsProtein phosphatase 1Site-directed mutagenesisActive site residuesOkadaic acidPhosphatase 1Calyculin AMammalian protein phosphatase 1PP-1Site residuesEnzyme activityMutation of residuesAmino acid residuesMechanism of catalysisActive siteInhibitor bindingAcid residuesInhibitory proteinMutationsResiduesMutagenesisDivalent cationsToxinY272Large lossesR221Characterization of the interaction between DARPP-32 and protein phosphatase 1 (PP-1): DARPP-32 peptides antagonize the interaction of PP-1 with binding proteins
Kwon Y, Huang H, Desdouits F, Girault J, Greengard P, Nairn A. Characterization of the interaction between DARPP-32 and protein phosphatase 1 (PP-1): DARPP-32 peptides antagonize the interaction of PP-1 with binding proteins. Proceedings Of The National Academy Of Sciences Of The United States Of America 1997, 94: 3536-3541. PMID: 9108011, PMCID: PMC20474, DOI: 10.1073/pnas.94.8.3536.Peer-Reviewed Original ResearchConceptsPP-1cPP-1C.PP-1DARPP-32Inhibitor 2Protein phosphatase 1Amino acid sequence analysisAmino acid residuesNH2-terminal regionAcid sequence analysisPhosphoinhibitor-1Threonine residuesPhosphatase 1Inhibitor-1Catalytic subunitCalyculin AOkadaic acidInhibitor proteinActive siteAcid residuesSequence analysisProteinEnzyme activityMotifResiduesCell cycle-dependent phosphorylation of mammalian protein phosphatase 1 by cdc2 kinase
Kwon Y, Lee S, Choi Y, Greengard P, Nairn A. Cell cycle-dependent phosphorylation of mammalian protein phosphatase 1 by cdc2 kinase. Proceedings Of The National Academy Of Sciences Of The United States Of America 1997, 94: 2168-2173. PMID: 9122166, PMCID: PMC20059, DOI: 10.1073/pnas.94.6.2168.Peer-Reviewed Original ResearchConceptsProtein phosphatase 1PP-1Phosphatase 1Cdc2 kinaseMammalian protein phosphatase 1Cell cycle-dependent phosphorylationCyclin-dependent protein kinase inhibitorEukaryotic cell cycle progressionCell synchronization studiesIntact mammalian cellsNormal cell divisionPP-1 activityCell fractionation studiesState of phosphorylationProtein kinase inhibitorsCell cycle progressionMammalian cellsCell divisionThr-320Cycle progressionMitotic cellsT320NIH 3T3PhosphorylationFractionation studies