Dpr Acts as a Molecular Switch, Inhibiting Wnt Signaling when Unphosphorylated, but Promoting Wnt Signaling when Phosphorylated by Casein Kinase Iδε 英文参考文献.docVIP

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Dpr Acts as a Molecular Switch, Inhibiting Wnt Signaling when Unphosphorylated, but Promoting Wnt Signaling when Phosphorylated by Casein Kinase Iδε 英文参考文献.doc

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Dpr Acts as a Molecular Switch, Inhibiting Wnt Signaling when Unphosphorylated, but Promoting Wnt Signaling when Phosphorylated by Casein Kinase Iδε 英文参考文献

DprActsasaMolecularSwitch,InhibitingWntSignaling whenUnphosphorylated,butPromotingWntSignaling whenPhosphorylatedbyCaseinKinaseId/e EvelynTeran,AronD.Branscomb¤,JoniM.Seeling* DepartmentofBiology,CityUniversityofNewYork,QueensCollege,Flushing,NewYork,UnitedStatesofAmerica Abstract TheWntpathwayisakeyregulatorofdevelopmentandtumorigenesis.Dpr(Dact/Frodo)influencesWntsignalinginpart throughtheinteractionofitsPDZ-BdomainwithDsh’sPDZdomain.StudieshaveshownthatXDpr1aanditscloserelative, Frodo,areinvolvedinmultiplestepsoftheWntpathwayineitherinhibitoryoractivatingroles.WefoundthatXDpr1ais phosphorylatedbycaseinkinaseId/e(CKId/e),anactivatorofWntsignaling,inthepresenceofXDsh.AbrogatingXDpr1a’s abilitytobindXDshthroughmutationofXDpr1a’sPDZ-BdomainblocksCK1d/e’sphosphorylationofXDpr1a.Conversely, XDshpossessingamutationinitsPDZdomainthatisunabletobindXDpr1adoesnotpromoteXDpr1aphosphorylation. PhosphorylationofXDpr1aandXDshbyCKId/edecreasestheirinteraction.Moreover,thephosphorylationofXDpr1aby CKId/e not only abrogates XDpr1a’s promotion of b-catenin degradation but blocks b-catenin degradation. Our data suggestthatXDpr1aphosphorylationbyCKId/eisdependentontheinteractionofXDpr1a’sPDZ-BdomainwithXDsh’sPDZ domain,andthatthephosphorylationstateofXDpr1adetermineswhetheritinhibitsoractivatesWntsignaling. Citation: Teran E, Branscomb AD, Seeling JM (2009) Dpr Acts as a Molecular Switch, Inhibiting Wnt Signaling when Unphosphorylated, but Promoting Wnt SignalingwhenPhosphorylatedbyCaseinKinaseId/e.PLoSONE4(5):e5522.doi:10.1371/journal.pone.0005522 Editor:WenqingXu,UniversityofWashington,UnitedStatesofAmerica ReceivedDecember15,2008;AcceptedApril20,2009;PublishedMay15,2009 Copyright: ? 2009 Teran et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricteduse,distribution,andreproductioninanymedium,providedtheoriginalauthorandsourcearecredited. Funding:Thisworkwas supported bygrantsfromNSF(MCB-0642067),NI