2003
Chapter 95 Atypical Protein Kinases The EF2/MHCK/ChaK Kinase Family
Nairn A. Chapter 95 Atypical Protein Kinases The EF2/MHCK/ChaK Kinase Family. 2003, 567-573. DOI: 10.1016/b978-012124546-7/50456-3.Peer-Reviewed Original ResearchProtein kinaseCatalytic domainAtypical protein kinaseProtein kinase AAnalysis of sequencesPhosphorylate serineAtypical kinaseProtein superfamiliesKinase familySignal transductionEvolutionary linkEnzyme classesSubstrate specificityKinase ADistinct membersTyrosine residuesMetabolic enzymesKinaseAmino acidsCatalytic mechanismIndividual functionsDetailed structural analysisEnzymeFamilyStructural features
1999
Mutation of Tyr307 and Leu309 in the Protein Phosphatase 2A Catalytic Subunit Favors Association with the α4 Subunit Which Promotes Dephosphorylation of Elongation Factor-2 †
Chung H, Nairn A, Murata K, Brautigan D. Mutation of Tyr307 and Leu309 in the Protein Phosphatase 2A Catalytic Subunit Favors Association with the α4 Subunit Which Promotes Dephosphorylation of Elongation Factor-2 †. Biochemistry 1999, 38: 10371-10376. PMID: 10441131, DOI: 10.1021/bi990902g.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAnion Exchange ResinsBacterial ProteinsCatalytic DomainChromatography, Ion ExchangeCOS CellsHemagglutininsLectinsLeucineMutagenesis, Site-DirectedOligopeptidesPeptide Elongation Factor 2Peptide Elongation FactorsPeptidesPhosphoprotein PhosphatasesPhosphoproteinsPhosphorylationPrecipitin TestsProtein Phosphatase 2Resins, SyntheticTransfectionTyrosineConceptsAlpha 4 proteinElongation factor 2AC dimerC subunitSpecific intracellular substratesProtein phosphatase 2ASites of phosphorylationAbc trimerCOS-7 cellsFactor 2B subunitC-terminal residuesTOR proteinsPhosphatase 2ANovel subunitCatalytic subunitTransient overexpressionSubstrate specificityCellular locationIntracellular substratesTransient expressionP70S6 kinaseSingle mutationProtein synthesisSubunitsCharacterization of the Neuronal Targeting Protein Spinophilin and Its Interactions with Protein Phosphatase-1 †
Hsieh-Wilson L, Allen P, Watanabe T, Nairn A, Greengard P. Characterization of the Neuronal Targeting Protein Spinophilin and Its Interactions with Protein Phosphatase-1 †. Biochemistry 1999, 38: 4365-4373. PMID: 10194355, DOI: 10.1021/bi982900m.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBinding SitesCell LineDopamine and cAMP-Regulated Phosphoprotein 32HumansMicrofilament ProteinsNerve Tissue ProteinsNeuronsPeptide FragmentsPeptidesPhosphoprotein PhosphatasesPhosphoproteinsProtein Phosphatase 1Protein Structure, TertiaryProteinsRabbitsSequence Homology, Amino AcidConceptsProtein phosphatase 1Ability of spinophilinPhosphatase 1PP1 regulatory subunitClass of proteinsAmino acids 447Cell cycle progressionPP1 activityPentapeptide motifRegulatory subunitCellular processesDeletion analysisDistinct subdomainsSubstrate specificityBinding domainsPhysiological substratesMutational analysisNeuronal proteinsProtein spinophilinCompetition binding assaysHigh-affinity binding domainsDARPP-32SpinophilinPostsynaptic densityBinding assays
1988
Protein kinases 1988: a current perspective
Blackshear P, Nairn A, Kuo J. Protein kinases 1988: a current perspective. The FASEB Journal 1988, 2: 2957-2969. PMID: 2972578, DOI: 10.1096/fasebj.2.14.2972578.Peer-Reviewed Original ResearchConceptsProtein tyrosine kinasesProtein kinaseIntrinsic protein tyrosine kinase activityProtein serine/threonine kinaseKinase activityTyrosine kinaseCalcium/calmodulin-dependent protein kinaseSerine/threonine kinaseCalmodulin-dependent protein kinaseProtein tyrosine kinase activityPhosphatidylinositol kinase activityNew enzyme speciesTyrosine kinase activityMyosin light chain kinaseCalmodulin kinase IIPseudosubstrate prototopeKinase IIIThreonine kinaseSignal transductionLight chain kinaseConstitutive inhibitorGrowth factor receptorKinase autophosphorylationSubstrate specificityCalcium-calmodulin kinase II
1985
Identification of calmodulin-dependent protein kinase III and its major Mr 100,000 substrate in mammalian tissues.
Nairn A, Bhagat B, Palfrey H. Identification of calmodulin-dependent protein kinase III and its major Mr 100,000 substrate in mammalian tissues. Proceedings Of The National Academy Of Sciences Of The United States Of America 1985, 82: 7939-7943. PMID: 3906654, PMCID: PMC390885, DOI: 10.1073/pnas.82.23.7939.Peer-Reviewed Original ResearchConceptsCaM-dependent protein kinaseCaM kinase IIIKinase IIIProtein kinaseMammalian tissuesCalmodulin-dependent protein kinase IIIProtein kinase IIIDependent protein kinaseProtein phosphorylation systemsWidespread tissue distributionTotal cytosolic proteinAnimal cellsPhosphorylation systemSubstrate specificityCytosolic proteinsMyosin light chainMajor substrateKinaseProteinSynapsin IPoor substrateCell linesPhosphorylase bMajor MrPolyclonal antibodies