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
1991
Evidence for isoproterenol-induced phosphorylation of phosphatase inhibitor-1 in the intact heart.
Neumann J, Gupta R, Schmitz W, Scholz H, Nairn A, Watanabe A. Evidence for isoproterenol-induced phosphorylation of phosphatase inhibitor-1 in the intact heart. Circulation Research 1991, 69: 1450-1457. PMID: 1659500, DOI: 10.1161/01.res.69.6.1450.Peer-Reviewed Original ResearchConceptsPhosphatase inhibitor-1Protein phosphatase inhibitor-1Type 1 phosphatase activityPhosphatase activityInhibitor-1Sodium dodecyl sulfate gelsDodecyl sulfate gelsIsoproterenol-induced phosphorylationSulfate gelsProteinRadioactive proteinsPhosphorylationPmol 32P/KdPhysiological bufferAntiserumActivityIndirect assayConcentrations of isoproterenolAgonist isoproterenolActivationAssaysVivoIntact heartCAMP