2022
Myosin light chain phosphatase catalytic subunit dephosphorylates cardiac myosin via mechanisms dependent and independent of the MYPT regulatory subunits
Lee E, Liu Z, Nguyen N, Nairn A, Chang AN. Myosin light chain phosphatase catalytic subunit dephosphorylates cardiac myosin via mechanisms dependent and independent of the MYPT regulatory subunits. Journal Of Biological Chemistry 2022, 298: 102296. PMID: 35872014, PMCID: PMC9418503, DOI: 10.1016/j.jbc.2022.102296.Peer-Reviewed Original ResearchConceptsMyosin light chain phosphataseRegulatory light chainRegulatory subunitCatalytic subunitPhosphatase catalytic subunitMain catalytic subunitSmooth muscle myosin light chain phosphataseNon-muscle cellsMuscle myosin light chain phosphataseMyosin regulatory light chainMyosin light chain kinaseLight chain kinasePP1cβTrimeric proteinConditional knockout miceLight chain phosphatasePhosphatase activitySubunitsPhosphate/Chain kinaseMuscle pathogenesisPhysiological regulationKnockout animalsMain isoformsProteinPP1cβ dephosphorylates cardiac myosin by MYPT‐dependent and independent mechanisms
Lee E, Liu Z, Nguyen N, Nairn A, Chang A. PP1cβ dephosphorylates cardiac myosin by MYPT‐dependent and independent mechanisms. The FASEB Journal 2022, 36 DOI: 10.1096/fasebj.2022.36.s1.r3877.Peer-Reviewed Original ResearchMyosin light chain phosphataseRegulatory light chainCardiac myosinSmooth muscleNormal cardiac functionMain catalytic subunitSmooth muscle contractionMyosin light chain kinaseMyosin phosphatase targetCardiac functionPP1cβLight chain kinaseCatalytic subunitAccessory subunitsConstitutive phosphorylationProtein stabilityLight chain phosphataseKnockout animalsMuscle contractionMuscle pathogenesisConditional knockoutCardiac muscle myosinCardiac myocytesCardiac musclePhosphatase activity
1996
Structure, 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
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
1984
The amino acid sequence of rabbit skeletal muscle calmodulin
Nairn A, Grand R, Perry S. The amino acid sequence of rabbit skeletal muscle calmodulin. FEBS Letters 1984, 167: 215-220. PMID: 6698209, DOI: 10.1016/0014-5793(84)80129-5.Peer-Reviewed Original ResearchConceptsSingle polypeptide chainMyosin light chain kinaseBlocked N terminusRabbit skeletal muscleLight chain kinasePhosphorylase kinaseMammalian calmodulinN-terminusPolypeptide chainResidues 48Chain kinaseAmide assignmentsCalmodulinLow ionic strength bufferKinaseSkeletal muscleIonic strength bufferSequenceN-terminal tripeptideStrength bufferTerminal tripeptideTerminusSubunitsProteinResidues
1980
The preparation of calmodulins from barley (Hordeum sp.) and basidiomycete fungi
Grand R, Nairn A, Perry S. The preparation of calmodulins from barley (Hordeum sp.) and basidiomycete fungi. Biochemical Journal 1980, 185: 755-760. PMID: 6248033, PMCID: PMC1161454, DOI: 10.1042/bj1850755.Peer-Reviewed Original ResearchConceptsRabbit skeletal muscle troponin ICalmodulin-like proteinPresence of Ca2Myosin light chain kinaseSkeletal muscle troponin IMammalian proteinsFungal calmodulinsLight chain kinaseMammalian calmodulinBovine brain calmodulinHigher fungiAmino acid analysisEscherichia coliCalmodulinProteinFungiE. coliAcid analysisBrain calmodulinElectrophoretic mobilityBarleyPolyacrylamide gelsM ureaColiNumber of differences
1979
Calmodulin and myosin light-chain kinase of rabbit fast skeletal muscle
Nairn A, Perry S. Calmodulin and myosin light-chain kinase of rabbit fast skeletal muscle. Biochemical Journal 1979, 179: 89-97. PMID: 224861, PMCID: PMC1186598, DOI: 10.1042/bj1790089.Peer-Reviewed Original Research