P130Cas Attenuates Epidermal Growth Factor (EGF) Receptor Internalization by Modulating EGF-Triggered Dynamin Phosphorylation 英文参考文献.docVIP

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P130Cas Attenuates Epidermal Growth Factor (EGF) Receptor Internalization by Modulating EGF-Triggered Dynamin Phosphorylation 英文参考文献.doc

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P130Cas Attenuates Epidermal Growth Factor (EGF) Receptor Internalization by Modulating EGF-Triggered Dynamin Phosphorylation 英文参考文献

P130CasAttenuatesEpidermalGrowthFactor(EGF) ReceptorInternalizationbyModulatingEGF-Triggered DynaminPhosphorylation YongSeokKang1,WookKim2,YunHyunHuh1,JeomilBae1,JinSooKim1,WooKeunSong1* 1DepartmentofLifeScience,BioImagingandCellDynamicsResearchCenter,GwangjuInstituteofScienceandTechnology,Gwangju,Korea,2DiabetesSection,National InstituteonAging,NationalInstitutesofHealth,Baltimore,Maryland,UnitedStatesofAmerica Abstract Background:Endocytosiscontrolslocalization-specificsignaltransductionviaepidermalgrowthfactorreceptor(EGFR),as wellasdownregulationofthatreceptor.Extracellularmatrix(ECM)-integrincouplinginducesformationofmacromolecular complexesthatincludeEGFR,integrin,Srckinaseandp130Cas,resultinginEGFRactivation.Inaddition,celladhesionto ECMincreasesEGFRlocalizationatthecellsurfaceandreducesEGFRinternalization.Themolecularmechanismsinvolved arenotyetwellunderstood. Methodology/Principal Findings: We investigated the molecular mechanism by which p130Cas affects the endocytic regulationofEGFR.Biochemicalquantificationrevealedthatcelladhesiontofibronectin(FN)increasestotalEGFRlevelsand itsphosphorylation,andthatp130Casisrequiredforthisprocess.MeasurementsofTexasRed-labeledEGFuptakeandcell surface EGFR revealed that p130Cas overexpression reduces EGF-induced EGFR internalization, while p130Cas depletion enhances it. In addition, both FN-mediated cell adhesion and p130Cas overexpression reduce EGF-stimulated dynamin phosphorylation, which is necessary for EGF-induced EGFR internalization. Coimmunoprecipitation and GST pull-down assaysconfirmedtheinteractionbetweenp130Casanddynamin.Moreover,aSH3-domain-deletedformofp130Cas,which shows diminished bindingto dynamin,inhibitsdynamin phosphorylation andEGF uptake less effectivelythanwild-type p130Cas. Conclusions/Significance:Ourresultsshowthatp130CasplaysaninhibitoryroleinEGFRinternalizationviaitsinteraction withdynamin.GiventhattheEGFRinternalizationprocessdeterminessignalingdensityandspecificityintheEGFRpathway, thesef