2010
Chapter 79 The EF2K/MHCK/TRPM7 Family of Atypical Protein Kinases
Wiseman S, Wei F, Nairn A. Chapter 79 The EF2K/MHCK/TRPM7 Family of Atypical Protein Kinases. 2010, 587-599. DOI: 10.1016/b978-0-12-374145-5.00079-6.Peer-Reviewed Original ResearchEF2KProtein synthesisElongation stepAtypical protein kinaseAtypical kinase familySpecific subcellular compartmentsCellular stress pathwaysLocal protein synthesisNeuronal growth conesActivity-dependent regulationKinase familySubcellular compartmentsCatalytic domainKinase domainProtein kinaseEnzymatic functionSecond messengerN-terminalK activityPhosphorylationStress pathwaysGrowth conesParticular Ca2EF2Regulation
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
2001
Opposing Changes in Phosphorylation of Specific Sites in Synapsin I During Ca2+-Dependent Glutamate Release in Isolated Nerve Terminals
Jovanovic J, Sihra T, Nairn A, Hemmings H, Greengard P, Czernik A. Opposing Changes in Phosphorylation of Specific Sites in Synapsin I During Ca2+-Dependent Glutamate Release in Isolated Nerve Terminals. Journal Of Neuroscience 2001, 21: 7944-7953. PMID: 11588168, PMCID: PMC6763853, DOI: 10.1523/jneurosci.21-20-07944.2001.Peer-Reviewed Original ResearchConceptsDependent dephosphorylationProtein phosphatase 2AMultiple protein kinasesPhosphorylation site 1Protein phosphatase 2BSynapsin IPhosphatase 2APhosphorylation sitesPhosphatase 2BSynapsin functionProtein kinaseDependent phosphorylationSynapsin I phosphorylationDephosphorylation processNeuronal phosphoproteinSynapsin I.Synaptic vesiclesCalcineurin activityPhosphorylationI phosphorylationDephosphorylationNeurotransmitter releaseSpecific sitesExcellent substrateSite 1Regulation of cyclin-dependent kinase 5 and casein kinase 1 by metabotropic glutamate receptors
Liu F, Ma X, Ule J, Bibb J, Nishi A, DeMaggio A, Yan Z, Nairn A, Greengard P. Regulation of cyclin-dependent kinase 5 and casein kinase 1 by metabotropic glutamate receptors. Proceedings Of The National Academy Of Sciences Of The United States Of America 2001, 98: 11062-11068. PMID: 11572969, PMCID: PMC58683, DOI: 10.1073/pnas.191353898.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCalcium ChannelsCasein KinasesCyclin-Dependent Kinase 5Cyclin-Dependent KinasesDopamine and cAMP-Regulated Phosphoprotein 32Enzyme InhibitorsIn Vitro TechniquesKineticsMaleMembrane PotentialsMethoxyhydroxyphenylglycolMiceMice, Inbred C57BLNeostriatumNerve Tissue ProteinsNeuronsPatch-Clamp TechniquesPhosphoproteinsPhosphorylationPhosphoserinePhosphothreonineProtein KinasesReceptors, Metabotropic GlutamateConceptsCasein kinase 1Cyclin-dependent kinase 5Ser-137Thr-75CK1 activityKinase 1Kinase 5DARPP-32Regulation of Cdk5Neuronal protein kinaseActivation of Cdk5Cellular functionsProtein kinaseDNA repairEnhanced phosphorylationFirst messengersCdk5 activitySpecific inhibitorCdk5Effects of DHPGMetabotropic glutamate receptorsNeurite outgrowthIC261Glutamate receptorsDHPG-induced increaseAngiotensin II regulates phosphorylation of translation elongation factor-2 in cardiac myocytes
Everett A, Stoops T, Nairn A, Brautigan D. Angiotensin II regulates phosphorylation of translation elongation factor-2 in cardiac myocytes. AJP Heart And Circulatory Physiology 2001, 281: h161-h167. PMID: 11406481, DOI: 10.1152/ajpheart.2001.281.1.h161.Peer-Reviewed Original ResearchMeSH KeywordsAngiotensin IIAnimalsCells, CulturedChromonesEnzyme InhibitorsMitogen-Activated Protein KinasesMorpholinesMyocardiumPeptide Elongation Factor 2Phosphoprotein PhosphatasesPhosphorylationProtein BiosynthesisProtein Phosphatase 2RatsRats, Sprague-DawleyReceptor, Angiotensin, Type 1Receptor, Angiotensin, Type 2Receptors, AngiotensinSignal TransductionSirolimusConceptsEukaryotic elongation factor 2Mitogen-activated protein kinaseElongation factor 2Protein phosphatase 2A inhibitor okadaic acidTranslation elongation factor 2Protein synthesisInhibitor okadaic acidFactor 2Rapamycin (mTOR) inhibitor rapamycinProtein translationDephosphorylated statePolypeptide elongationII-dependent increaseProtein kinaseEEF2 kinaseOkadaic acidDependent regulationInhibitor FK506MAPK activationPD 98059Cardiac myocytesDephosphorylationInhibitor rapamycinNeonatal cardiac myocytesRat neonatal cardiac myocytesCrystal Structure of the Atypical Protein Kinase Domain of a TRP Channel with Phosphotransferase Activity
Yamaguchi H, Matsushita M, Nairn A, Kuriyan J. Crystal Structure of the Atypical Protein Kinase Domain of a TRP Channel with Phosphotransferase Activity. Molecular Cell 2001, 7: 1047-1057. PMID: 11389851, DOI: 10.1016/s1097-2765(01)00256-8.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid MotifsAmino Acid SequenceAnimalsBinding SitesCalcium ChannelsCrystallography, X-RayCyclic AMP-Dependent Protein KinasesEvolution, MolecularMiceModels, MolecularMolecular Sequence DataNucleotidesPhosphotransferasesProtein Structure, SecondaryProtein Structure, TertiarySequence AlignmentTRPC Cation ChannelsZincConceptsEukaryotic protein kinasesProtein kinaseTransient receptor potential channelsCatalytic domainKinase domainProtein kinase domainKinase catalytic domainDetectable sequence similarityATP-grasp domainEukaryotic cellsThreonine residuesSequence similarityChannel kinaseSequence comparisonCatalytic corePotential channelsMetabolic enzymesPhosphotransferase activityKinaseChannel functionTRP channelsExternal signalsUnexpected similaritiesWide distributionProteinAuto‐inhibition of Ca2+/calmodulin‐dependent protein kinase II by its ATP‐binding domain
Lengyel I, Nairn A, McCluskey A, Tóth G, Penke B, Rostas J. Auto‐inhibition of Ca2+/calmodulin‐dependent protein kinase II by its ATP‐binding domain. Journal Of Neurochemistry 2001, 76: 1066-1072. PMID: 11181826, DOI: 10.1046/j.1471-4159.2001.00139.x.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAnimalsBinding SitesCalcium-Calmodulin-Dependent Protein Kinase Type 1Calcium-Calmodulin-Dependent Protein Kinase Type 2Calcium-Calmodulin-Dependent Protein Kinase Type 4Calcium-Calmodulin-Dependent Protein KinasesCyclic AMP-Dependent Protein KinasesDose-Response Relationship, DrugEnzyme ActivationEnzyme InhibitorsPeptide FragmentsPeptidesProtein Structure, TertiaryRatsSubstrate SpecificityConceptsATP-binding domainDependent protein kinase IIProtein kinase IIProtein kinaseCaMPK-IIKinase IICAMP-dependent protein kinaseDependent protein kinaseSubstitution of phenylalaninePhysiological processesKey enzymeAutocamtide-2Position 25Phenylalanine 25Molecular interactionsKinasePeptide fragmentsDependent activityIndependent activityATPEnzymeCrucial roleIntramolecular interactionsDomainInhibitionPhosphorylation of Protein Phosphatase Inhibitor-1 by Cdk5*
Bibb J, Nishi A, O'Callaghan J, Ule J, Lan M, Snyder G, Horiuchi A, Saito T, Hisanaga S, Czernik A, Nairn A, Greengard P. Phosphorylation of Protein Phosphatase Inhibitor-1 by Cdk5*. Journal Of Biological Chemistry 2001, 276: 14490-14497. PMID: 11278334, DOI: 10.1074/jbc.m007197200.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBinding SitesBrainCalcineurinCarrier ProteinsCDC2 Protein KinaseCyclic AMPCyclic AMP-Dependent Protein KinasesCyclin-Dependent Kinase 5Cyclin-Dependent KinasesGlutamic AcidIntracellular Signaling Peptides and ProteinsKineticsMiceMice, Inbred C57BLMutagenesis, Site-DirectedN-MethylaspartatePhosphoprotein PhosphatasesPhosphorylationProlineProtein Phosphatase 1RabbitsRatsRecombinant ProteinsRNA-Binding ProteinsSerineTime FactorsConceptsProtein phosphatase inhibitor-1Protein phosphatase 1Phosphatase inhibitor-1Ser-67Protein kinasePhosphatase 1CAMP-dependent protein kinase resultsSelective protein kinase inhibitorsCAMP-dependent protein kinaseProtein phosphatase 2AProline-directed kinasesMitogen-activated protein kinaseInhibitor-1Protein kinase resultsSignal transduction eventsPhosphorylation state-specific antibodiesCAMP-dependent protein kinase activationState of phosphorylationProtein kinase inhibitorsProtein kinase activationPhosphatase 2AThr-35Protein phosphatasePhosphorylation sitesGlutamate-dependent regulationDecreased levels of ARPP-19 and PKA in brains of Down syndrome and Alzheimer’s disease
Kim S, Nairn A, Cairns N, Lubec G. Decreased levels of ARPP-19 and PKA in brains of Down syndrome and Alzheimer’s disease. Journal Of Neural Transmission. Supplementa 2001, 263-272. PMID: 11771749, DOI: 10.1007/978-3-7091-6262-0_21.Peer-Reviewed Original ResearchConceptsARPP-19Protein kinaseDifferential display polymerase chain reactionAlzheimer's diseaseDown syndromeCAMP-dependent protein kinaseTemporal cortexActivity of PKASignal transductionDownregulated sequenceBrain regionsNeurodegenerative disordersDiseaseImpaired mechanismsProtein levelsDecreased activityChain reactionFirst evidenceSignificant reductionSyndromeCortexDisordersTransductionHomologyKinase
2000
Amplification of dopaminergic signaling by a positive feedback loop
Nishi A, Bibb J, Snyder G, Higashi H, Nairn A, Greengard P. Amplification of dopaminergic signaling by a positive feedback loop. Proceedings Of The National Academy Of Sciences Of The United States Of America 2000, 97: 12840-12845. PMID: 11050161, PMCID: PMC18851, DOI: 10.1073/pnas.220410397.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCalcineurinCocaineCyclic AMP-Dependent Protein KinasesCyclin-Dependent Kinase 5Cyclin-Dependent KinasesDopamineDopamine and cAMP-Regulated Phosphoprotein 32FeedbackIn Vitro TechniquesMiceMice, Inbred C57BLNeostriatumNerve Tissue ProteinsPhosphoprotein PhosphatasesPhosphoproteinsPhosphorylationProtein Phosphatase 2Receptors, Dopamine D1Receptors, Dopamine D2Signal TransductionConceptsState of phosphorylationProtein kinaseThr-75Protein phosphatase 2A activityCAMP-dependent protein kinasePhosphatase 2A activityCyclin-dependent kinase 5DARPP-32Dopamine D1 receptor-mediated activationDopamine D2 receptor stimulationStriatal DARPP-32Receptor-mediated activationD2 receptor stimulationAction of dopamineEffects of dopaminePositive feedback loopPKA signalingKinase 5Inhibitory constraintPhosphorylationAcute cocaineWhole animalNeostriatal slicesReceptor stimulationDopaminergic signalingThe Dopamine/D1 Receptor Mediates the Phosphorylation and Inactivation of the Protein Tyrosine Phosphatase STEP via a PKA-Dependent Pathway
Paul S, Snyder G, Yokakura H, Picciotto M, Nairn A, Lombroso P. The Dopamine/D1 Receptor Mediates the Phosphorylation and Inactivation of the Protein Tyrosine Phosphatase STEP via a PKA-Dependent Pathway. Journal Of Neuroscience 2000, 20: 5630-5638. PMID: 10908600, PMCID: PMC6772528, DOI: 10.1523/jneurosci.20-15-05630.2000.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAnimalsCatalytic DomainCorpus StriatumCyclic AMP-Dependent Protein KinasesEnzyme ActivationIn Vitro TechniquesMaleMolecular Sequence DataNeuronsPhosphoproteinsPhosphorus RadioisotopesPhosphorylationProtein Tyrosine PhosphatasesProtein Tyrosine Phosphatases, Non-ReceptorRatsRats, Sprague-DawleyReceptors, Dopamine D1Signal TransductionConceptsProtein tyrosine phosphatase familyCAMP-dependent protein kinaseTryptic phosphopeptide mappingPotential phosphorylation sitesUnique N-terminalProtein-protein interactionsMembrane-associated proteinsRole of phosphorylationTyrosine phosphatase familyAmino acid sequenceSite-directed mutagenesisAmino acid sequencingPKA-dependent pathwayTyrosine phosphatase STEPPhosphatase familyPhosphopeptide mappingPhosphorylation sitesAlternative splicingSubcellular compartmentsProtein kinaseTerminal domainEquivalent residuesCytosolic proteinsSpecific residuesAcid sequenceNovel compounds, ‘1,3-selenazine derivatives’ as specific inhibitors of eukaryotic elongation factor-2 kinase
Cho S, Koketsu M, Ishihara H, Matsushita M, Nairn A, Fukazawa H, Uehara Y. Novel compounds, ‘1,3-selenazine derivatives’ as specific inhibitors of eukaryotic elongation factor-2 kinase. Biochimica Et Biophysica Acta 2000, 1475: 207-215. PMID: 10913818, DOI: 10.1016/s0304-4165(00)00061-1.Peer-Reviewed Original ResearchConceptsV-src-transformed NIH3T3 cellsEukaryotic elongation factor 2 kinaseProtein kinase AElongation factor 2 kinaseProtein kinase CProtein tyrosine kinasesEEF-2KProtein kinaseEEF-2K inhibitorNIH3T3 cellsCalmodulin-dependent protein kinaseV-Src kinaseMultiple protein kinasesCalmodulin-dependent protein kinase IIProtein levelsK inhibitorsProtein kinase IIEEF-2K.Kinase AKinase IITyrosine kinaseKinase CKinaseTs-4Specific inhibitorRegulation of Phosphorylation of the GluR1 AMPA Receptor in the Neostriatum by Dopamine and Psychostimulants In Vivo
Snyder G, Allen P, Fienberg A, Valle C, Huganir R, Nairn A, Greengard P. Regulation of Phosphorylation of the GluR1 AMPA Receptor in the Neostriatum by Dopamine and Psychostimulants In Vivo. Journal Of Neuroscience 2000, 20: 4480-4488. PMID: 10844017, PMCID: PMC6772453, DOI: 10.1523/jneurosci.20-12-04480.2000.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBenzazepinesCentral Nervous System StimulantsDopamineDopamine and cAMP-Regulated Phosphoprotein 32In Vitro TechniquesMaleMethamphetamineMiceMice, Inbred C57BLMice, KnockoutMicrowavesNeostriatumNerve Tissue ProteinsOkadaic AcidPhosphoprotein PhosphatasesPhosphoproteinsPhosphorylationProtein Phosphatase 1Protein Phosphatase 2Receptors, AMPAReceptors, Dopamine D1Receptors, Dopamine D2Recombinant Fusion ProteinsSerineConceptsCAMP-dependent protein kinaseProtein phosphatase 2A.AMPA-type glutamate receptorsCalmodulin-dependent kinase IICalcium/calmodulin-dependent kinase IIRegulation of phosphorylationProtein kinase CPhosphatase 2A.Protein kinaseKinase IIPhosphorylation of GluR1Kinase CGluR1 AMPA receptorsPhosphorylationCellular effectorsGlutamate receptorsDARPP-32Physiological activityAMPA receptorsPsychostimulant cocaineChannel conductanceReceptorsD1-type dopamine receptorsActivationVivo
1999
Phosphorylation of DARPP-32 by Cdk5 modulates dopamine signalling in neurons
Bibb J, Snyder G, Nishi A, Yan Z, Meijer L, Fienberg A, Tsai L, Kwon Y, Girault J, Czernik A, Huganir R, Hemmings H, Nairn A, Greengard P. Phosphorylation of DARPP-32 by Cdk5 modulates dopamine signalling in neurons. Nature 1999, 402: 669-671. PMID: 10604473, DOI: 10.1038/45251.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCDC2 Protein KinaseCyclic AMP-Dependent Protein KinasesCyclin-Dependent Kinase 5Cyclin-Dependent KinasesDopamineDopamine and cAMP-Regulated Phosphoprotein 32Enzyme InhibitorsIn Vitro TechniquesMiceNerve Tissue ProteinsNeuronsPhosphoproteinsPhosphorylationRecombinant ProteinsSignal TransductionThreonineConceptsProtein kinase APhospho-ThrDARPP-32Serine/threonine phosphataseSerine/threonine kinaseInhibitor of PKAProtein phosphatase 1Signal transduction moleculesParticular amino acid residuesSignal transduction mechanismsAmino acid residuesCyclin-dependent kinase 5Threonine phosphataseThreonine 75PKA substratesThreonine kinasePhosphatase 1Phosphatase inhibitorProtein kinaseTransduction moleculesKinase ASingle proteinKinase 5Transduction mechanismsKinaseRole of Calcineurin and Protein Phosphatase‐2A in the Regulation of DARPP‐32 Dephosphorylation in Neostriatal Neurons
Nishi A, Snyder G, Nairn A, Greengard P. Role of Calcineurin and Protein Phosphatase‐2A in the Regulation of DARPP‐32 Dephosphorylation in Neostriatal Neurons. Journal Of Neurochemistry 1999, 72: 2015-2021. PMID: 10217279, DOI: 10.1046/j.1471-4159.1999.0722015.x.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCalcineurinCalcineurin InhibitorsCyclosporineDopamine and cAMP-Regulated Phosphoprotein 32Drug CombinationsDrug SynergismEnzyme InhibitorsIn Vitro TechniquesMaleMarine ToxinsMiceMice, Inbred C57BLNeostriatumNerve Tissue ProteinsNeuronsOkadaic AcidOxazolesPhosphoprotein PhosphatasesPhosphoproteinsPhosphorylationProtein Phosphatase 1Protein Phosphatase 2ConceptsProtein phosphatase 1Protein phosphatase 2AOkadaic acidPhosphorylated DARPP-32DARPP-32 phosphorylationPhosphatase 2APP-2ADARPP-32Cyclic AMP-dependent protein kinaseAMP-dependent protein kinasePP-2A activityRole of calcineurinPhosphatase 1Calyculin AMouse neostriatal slicesProtein kinaseAction of cyclosporinDependent activationCalcineurinPresence of cyclosporinPhosphorylationDephosphorylationSynergistic increaseThr34Potent inhibitorPhosphorylation of the Cytoplasmic Domain of Alzheimer's β-Amyloid Precursor Protein at Ser655 by a Novel Protein Kinase
Isohara T, Horiuchi A, Watanabe T, Ando K, Czernik A, Uno I, Greengard P, Nairn A, Suzuki T. Phosphorylation of the Cytoplasmic Domain of Alzheimer's β-Amyloid Precursor Protein at Ser655 by a Novel Protein Kinase. Biochemical And Biophysical Research Communications 1999, 258: 300-305. PMID: 10329382, DOI: 10.1006/bbrc.1999.0637.Peer-Reviewed Original ResearchConceptsNovel protein kinaseAlzheimer's beta-amyloid precursor proteinProtein kinase CExtracellular signal-regulated kinaseProtein kinaseCytoplasmic domainCalmodulin-dependent protein kinase IIΒ-amyloid precursor proteinPrecursor proteinAlzheimer's β-Amyloid Precursor ProteinSignal-regulated kinaseProtein kinase IIBeta-amyloid precursor proteinKinase IUnidentified proteinsKinase IIKinase CKinaseSer655ProteinAlzheimer's diseaseThr654Rat brainPhosphorylationDomainPhylogenetically conserved CK‐II phosphorylation site of the murine homeodomain protein Hoxb‐6
Fienberg A, Nordstedt C, Belting H, Czernik A, Nairn A, Gandy S, Greengard P, Ruddle F. Phylogenetically conserved CK‐II phosphorylation site of the murine homeodomain protein Hoxb‐6. Journal Of Experimental Zoology 1999, 285: 76-84. PMID: 10327653, DOI: 10.1002/(sici)1097-010x(19990415)285:1<76::aid-jez9>3.0.co;2-k.Peer-Reviewed Original ResearchConceptsTwo-dimensional tryptic phosphopeptide mappingTryptic phosphopeptide mappingHoxb-6Casein kinase IIHomeodomain proteinsPhosphopeptide mappingPhosphorylation sitesHoxc-8Protein kinaseSf9 cellsCasein kinase II phosphorylation sitesKinase IICK-II phosphorylation sitesCAMP-dependent protein kinaseSignal transduction mechanismsBaculovirus expression systemProtein functionPhosphorylation stateMouse embryonic spinal cordExpression systemSerine 214Embryonic spinal cordTransduction mechanismsKinaseProteinInhibition of the Ca2+/Calmodulin-dependent Protein Kinase I Cascade by cAMP-dependent Protein Kinase*
Matsushita M, Nairn A. Inhibition of the Ca2+/Calmodulin-dependent Protein Kinase I Cascade by cAMP-dependent Protein Kinase*. Journal Of Biological Chemistry 1999, 274: 10086-10093. PMID: 10187789, DOI: 10.1074/jbc.274.15.10086.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCalcium-Calmodulin-Dependent Protein Kinase KinaseCalcium-Calmodulin-Dependent Protein Kinase Type 1Calcium-Calmodulin-Dependent Protein Kinase Type 4Calcium-Calmodulin-Dependent Protein KinasesCyclic AMP-Dependent Protein KinasesFeedbackHippocampusPC12 CellsPeptide MappingPhosphorylationProtein Serine-Threonine KinasesRatsSubstrate SpecificityConceptsActivation of PKACAMP-dependent protein kinaseDependent protein kinase IProtein kinaseProtein kinase IThreonine 108Kinase ITwo-dimensional phosphopeptide mappingDependent signal transduction pathwaysInhibition of CaMKKSignal transduction pathwaysIntact PC12 cellsRegulatory phosphorylationPhosphopeptide mappingTransduction pathwaysCaMKI activityCaMKKIntact cellsPhosphorylationPC12 cellsKinaseNegative feedback mechanismEnzyme cascadeEnzyme activityRapid inhibition
1996
cGMP-Dependent Protein Kinase in Dorsal Root Ganglion: Relationship with Nitric Oxide Synthase and Nociceptive Neurons
Qian Y, Chao D, Santillano D, Cornwell T, Nairn A, Greengard P, Lincoln T, Bredt D. cGMP-Dependent Protein Kinase in Dorsal Root Ganglion: Relationship with Nitric Oxide Synthase and Nociceptive Neurons. Journal Of Neuroscience 1996, 16: 3130-3138. PMID: 8627352, PMCID: PMC6579134, DOI: 10.1523/jneurosci.16-10-03130.1996.Peer-Reviewed Original ResearchConceptsNeuronal nitric oxide synthaseCGMP-dependent protein kinaseNitric oxide synthaseSensory neuronsProtein kinase ICGMP-dependent protein kinase IOxide synthaseKinase IEmbryonic developmentProtein kinaseG-substrateCalcitonin gene-related polypeptideMedium-diameter DRG neuronsPeripheral nerve axotomyInfluences plasticityDorsal root gangliaCGMP actionRoof plateNerve axotomyDRG neuronsNociceptive neuronsNociceptive processingRoot gangliaSubstance PSpinal cordStructure, Regulation, and Function of Calcium/Calmodulin-Dependent Protein Kinase I
Picciotto M, Nastiuk K, Nairn A. Structure, Regulation, and Function of Calcium/Calmodulin-Dependent Protein Kinase I. Advances In Pharmacology 1996, 36: 251-275. PMID: 8783563, DOI: 10.1016/s1054-3589(08)60585-2.Peer-Reviewed Original ResearchConceptsProtein kinaseProtein kinase CMyosin light chain kinaseKinase ICaM kinaseSecond messenger-regulated protein kinasesCalmodulin-dependent protein kinase ICalcium/calmodulin-dependent protein kinase ICAMP-dependent protein kinaseSpecific subcellular locationsMultifunctional protein kinaseTerminal regulatory domainDependent protein kinaseCaM kinase familyClass of enzymesProtein kinase ICaM kinase IAmino acid residuesMyosin P-light chainDomain bindsAutoinhibitory mechanismRegulatory domainKinase familyProtein phosphorylationLight chain kinase