Protein Kinase C-Dependent Dephosphorylation of Tyrosine Hydroxylase Requires the B56δ Heterotrimeric Form of Protein Phosphatase 2A 英文参考文献.docVIP

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Protein Kinase C-Dependent Dephosphorylation of Tyrosine Hydroxylase Requires the B56δ Heterotrimeric Form of Protein Phosphatase 2A 英文参考文献.doc

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Protein Kinase C-Dependent Dephosphorylation of Tyrosine Hydroxylase Requires the B56δ Heterotrimeric Form of Protein Phosphatase 2A 英文参考文献

ProteinKinaseC-DependentDephosphorylationof TyrosineHydroxylaseRequirestheB56dHeterotrimeric FormofProteinPhosphatase2A Jung-HyuckAhn1*,YongKim2,Hee-SunKim3,PaulGreengard2,AngusC.Nairn2,4* 1DepartmentofBiochemistry,EwhaWomansUniversitySchoolofMedicine,Seoul,Korea,2LaboratoryofMolecularandCellularNeuroscience,TheRockefellerUniversity, NewYork,NewYork,UnitedStatesofAmerica,3DepartmentofMolecularMedicineandTissueInjuryDefenseResearchCenter,EwhaWomansUniversity, Schoolof Medicine,Seoul,Korea,4DepartmentofPsychiatry,YaleUniversitySchoolofMedicine,NewHaven,Connecticut,UnitedStatesofAmerica Abstract Tyrosine hydroxylase, which plays a critical role in regulation of dopamine synthesis, is known to be controlled by phosphorylation at several critical sites. One of these sites, Ser40, is phosphorylated by a number of protein kinases, includingproteinkinaseA.ThemajorproteinphosphatasethatdephosphorylatesSer40isproteinphosphatase-2A(PP2A). ArecentstudyhasalsolinkedproteinkinaseCtothedephosphorylationofSer40[1],butthemechanismisunclear.PP2A isoforms are comprised of catalytic, scaffold, and regulatory subunits, the regulatory B subunits being able to influence cellularlocalizationandsubstrateselection.Inthecurrentstudy,wefindthatproteinkinaseCisabletophosphorylateakey regulatorysiteintheB56dsubunitleadingtoactivationofPP2A.Inturn,activationoftheB56d-containingheterotrimeric formofPP2AisresponsibleforenhanceddephosphorylationofSer40oftyrosinehydroylaseinresponsetostimulationof PKC. In support of this mechanism, down-regulation of B56d expression in N27 cells using RNAi was found to increase dopaminesynthesis.TogetherthesestudiesrevealmoleculardetailsofhowproteinkinaseCislinkedtoreducedtyrosine hydroxylaseactivityviacontrolofPP2A,andalsoaddtothecomplexityofproteinkinase/proteinphosphataseinteractions. Citation: Ahn J-H,Kim Y,KimH-S,GreengardP,Nairn AC(2011) Protein KinaseC-DependentDephosphorylation ofTyrosine Hydroxylase Requires theB56d HeterotrimericFormofProte