Role of Monoubiquitylation on the Control of IκBα Degradation and NF-κB Activity 英文参考文献.docVIP

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Role of Monoubiquitylation on the Control of IκBα Degradation and NF-κB Activity 英文参考文献.doc

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Role of Monoubiquitylation on the Control of IκBα Degradation and NF-κB Activity 英文参考文献

RoleofMonoubiquitylationontheControlofIkBa DegradationandNF-k BActivity ElisaDaSilva-Ferrada1,Mo′nicaTorres-Ramos1¤,FabienneAillet1,MichelaCampagna2,CarlosMatute3, CarmenRivas2,ManuelS.Rodr?′guez1,4*,Vale′rieLang1 1ProteomicsUnit,CICbioGUNE,CIBERehd,BizkaiaTechnologyPark,Derio,Spain,2CentroNacionaldeBiotecnolog?′a,CSIC,CampusUniversidadAuto′nomadeMadrid, Madrid,Spain,3DepartmentofNeuroscienceUniversityoftheBasqueCountryUPV/EHU,CIBERNED,Leioa,Bizkaia,Spain,4DepartmentofBiochemistryUniversityofthe BasqueCountryUPV/EHU,Leioa,Bizkaia,Spain Abstract TheNF-kBpathwayisregulatedbymultiplepost-translationalmodificationsincludingphosphorylation,ubiquitylationand SUMOylation. Many of these modifications act on the natural inhibitor IkBa modulating its capacity to control signal- mediated NF-kB activity. While the canonical pathway involving the phosphorylation and polyubiquitylation of IkBa has beenwellcharacterized,theroleofthesepost-translationalmodificationsinthecontrolofbasalNF-kBactivityhasnotbeen deeplyexplored.UsingtherecentlydevelopedTandem-repeatedUbiquitinBindingEntities(alsoknownasubiquitintraps) tocaptureubiquitylatedproteins,weidentifiedmonoubiquitylatedformsofIkBafrommultipleratorgansandcelltypes. The identification of these forms was demonstrated through different procedures such as immunoprecipitations with specificubiquitinantibodiesorHis6-Ubiquitinpulldowns.MonoubiquitylatedformsofIkBaareresistanttoTNFa-mediated degradation and can be captured using TUBEs, even after proteasome inhibitors treatment. As it occurs for monoSUMOylation, monoubiquitylation is not dependent of the phosphorylation of IkBa on the serines 32/36 and is notoptimallydegradedafterTNFastimulation.Aubiquitin-IkBafusionexhibitsphosphorylationdefectsandresistanceto TNFa mediated degradation similar to the ones observed for endogenous monoubiquitylated IkBa. The N-terminal attachmentofasingleubiquitinmoietyontheIkBafusionresultsinadeficientbindingtotheIKKbkinaseandrecruitment oftheSCFlig