Cellular Prion Protein and Caveolin-1 Interaction in a Neuronal Cell Line Precedes FynErk 12 Signal Transduction英文文献资料.docVIP

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Cellular Prion Protein and Caveolin-1 Interaction in a Neuronal Cell Line Precedes FynErk 12 Signal Transduction英文文献资料.doc

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Cellular Prion Protein and Caveolin-1 Interaction in a Neuronal Cell Line Precedes FynErk 12 Signal Transduction英文文献资料

HindawiPublishingCorporation JournalofBiomedicineandBiotechnology Volume2006,ArticleID69469,Pages1–13 DOI10.1155/JBB/2006/69469 ResearchArticle CellularPrionProteinandCaveolin-1InteractioninaNeuronal CellLinePrecedesFyn/Erk1/2SignalTransduction MattiaToni,1EnzoSpisni,1CristianaGriffoni,1SpartacoSanti,2MassimoRiccio,2 PatriziaLenaz,1andVittorioTomasi1 1 2 DepartmentofExperimentalBiology,UniversityofBologna,ViaSelmi3,40126Bologna,Italy NationalResearchCouncil,InstituteofCytomorphology,40136Bologna,Italy Received7September2005;Revised23January2006;Accepted29January2006 Ithasbeenreportedthatcellularprionprotein(PrPc)isenrichedincaveolaeorcaveolae-likedomainswithcaveolin-1(Cav-1) participatingtosignaltransductioneventsbyFynkinaserecruitment.ByusingtheGlutathione-S-transferase(GST)-fusionpro- teinsassay,weobservedthatPrPcstronglyinteractsinvitrowithCav-1.Thus,weascertainedthePrPccaveolarlocalizationina hypothalamicneuronalcellline(GN11),byconfocalmicroscopyanalysis,?otationondensitygradient,andcoimmunoprecipita- tionexperiments.Followingtheanti-PrPcantibody-mediatedstimulationofliveGN11cells,weobservedthatPrPcclusteredon plasmamembranedomainsrichinCav-1inwhichFynkinaseconvergedtobeactivated.Aftertheseevents,asignalingcascade throughp42/44MAPkinase(Erk1/2)wastriggered,suggestingthatfollowingtranslocationsfromraftstocaveolaeorcaveolae- likedomainsPrPccouldinteractwithCav-1andinducesignaltransductionevents. Copyright?2006MattiaTonietal.ThisisanopenaccessarticledistributedundertheCreativeCommonsAttributionLicense, whichpermitsunrestricteduse,distribution,andreproductioninanymedium,providedtheoriginalworkisproperlycited. INTRODUCTION repeats highly conserved during evolution that are bind- ingsitesforcopperions[9].Inneuroblastomacellslacking caveolae,PrPchasbeenisolatedindetergent-insolublecom- plexesdenominated“caveolae-likedomains”(CLDs)andit hasbeenhypothesizedthatPrPcconversioninitspatholog- icalconformerPrPscrapie(PrPsc)occursinthissubcellu- larcompartment[10,11].Recent