2001
Protein phosphatase 1 regulation by inhibitors and targeting subunits
Watanabe T, Huang H, Horiuchi A, da Cruze Silva E, Hsieh-Wilson L, Allen P, Shenolikar S, Greengard P, Nairn A. Protein phosphatase 1 regulation by inhibitors and targeting subunits. Proceedings Of The National Academy Of Sciences Of The United States Of America 2001, 98: 3080-3085. PMID: 11248035, PMCID: PMC30610, DOI: 10.1073/pnas.051003898.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsCell LineChromosomal Proteins, Non-HistoneDNA-Binding ProteinsDopamine and cAMP-Regulated Phosphoprotein 32Enzyme InhibitorsGene ExpressionHistone ChaperonesMicrofilament ProteinsMolecular Sequence DataMyelin Basic ProteinNerve Tissue ProteinsPhosphoprotein PhosphatasesPhosphoproteinsProtein Phosphatase 1ProteinsRabbitsRecombinant Fusion ProteinsSpodopteraSubstrate SpecificityTranscription FactorsConceptsProtein phosphatase 1Native protein phosphatase-1PP1 nuclear targeting subunitPhosphotyrosine-containing substratesInhibitor 2Protein phosphatase 1 regulationRecombinant protein phosphatase 1Sf9 insect cellsC-terminal sequencesLoss of interactionTargeting subunitPP1/Phosphatase 1Insect cellsResidues 274Inhibitor proteinRecombinant proteinsProtein inhibitorSubunitsEscherichia coliY272Corresponding regionPhosphorylase a.MutationsRegulation
2000
Severed Molecules Functionally Define the Boundaries of the Cystic Fibrosis Transmembrane Conductance Regulator's Nh2-Terminal Nucleotide Binding Domain
Chan K, Csanády L, Seto-Young D, Nairn A, Gadsby D. Severed Molecules Functionally Define the Boundaries of the Cystic Fibrosis Transmembrane Conductance Regulator's Nh2-Terminal Nucleotide Binding Domain. The Journal Of General Physiology 2000, 116: 163-180. PMID: 10919864, PMCID: PMC2229491, DOI: 10.1085/jgp.116.2.163.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine MonophosphateAnimalsCystic Fibrosis Transmembrane Conductance RegulatorEndoplasmic ReticulumEpitopesFemaleGene DeletionGene ExpressionIon Channel GatingKineticsMembrane PotentialsMolecular Sequence DataMutagenesisOligopeptidesOocytesPatch-Clamp TechniquesPeptide FragmentsPeptidesPrecipitin TestsProtein BindingProtein Structure, TertiarySequence Homology, Amino AcidTransfectionXenopus laevisConceptsR domainCFTR channelsCOOH terminusMature formFull-length CFTRCystic fibrosis transmembrane conductance regulatorAmino acids 590Nucleotide Binding DomainFibrosis transmembrane conductance regulatorExcised patch recordingsChannel activityFamily of ATPRequirement of phosphorylationCFTR channel activityTransmembrane conductance regulatorNBD1 domainSmaller single-channel conductanceCFTR polypeptideTransmembrane domainATP bindingRegulatory domainCassette proteinNBD structuresNBD1Binding domains
1998
Isolation and Characterization of PNUTS, a Putative Protein Phosphatase 1 Nuclear Targeting Subunit*
Allen P, Kwon Y, Nairn A, Greengard P. Isolation and Characterization of PNUTS, a Putative Protein Phosphatase 1 Nuclear Targeting Subunit*. Journal Of Biological Chemistry 1998, 273: 4089-4095. PMID: 9461602, DOI: 10.1074/jbc.273.7.4089.Peer-Reviewed Original ResearchConceptsPhosphatase 1 nuclear targeting subunitProtein phosphatase 1Targeting subunitPP1 catalytic activityMammalian cell lysatesTwo-hybrid assayPP1 functionsNuclear functionsNuclear compartmentalizationNovel proteinPhosphatase 1Subcellular localizationCell physiologyCell lysatesCell nucleiSubunitsExogenous substratesInitial characterizationProteinStable complexesPotent modulationChromatinCloningMitosisCompartmentalization