Multisite Phosphorylation of the Guanine Nucleotide Exchange Factor Cdc24 during Yeast Cell Polarization 英文参考文献.docVIP

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Multisite Phosphorylation of the Guanine Nucleotide Exchange Factor Cdc24 during Yeast Cell Polarization 英文参考文献.doc

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Multisite Phosphorylation of the Guanine Nucleotide Exchange Factor Cdc24 during Yeast Cell Polarization 英文参考文献

MultisitePhosphorylationoftheGuanineNucleotide ExchangeFactorCdc24duringYeastCellPolarization StephanieC.Wai1,2,ScottA.Gerber3¤,RongLi1,4* 1StowersInstituteforMedicalResearch,KansasCity,Missouri,UnitedStatesofAmerica,2BiologicalandBiomedicalSciencesGraduateProgram,HarvardMedicalSchool, Boston,Massachusetts,UnitedStatesofAmerica,3DepartmentofCellBiology,HarvardMedicalSchool,Boston,Massachusetts,UnitedStatesofAmerica,4Departmentof MolecularandIntegrativePhysiology,UniversityofKansasMedicalCenter,KansasCity,Kansas,UnitedStatesofAmerica Abstract Background: Cell polarization is essential for processes such as cell migration and asymmetric cell division. A common regulator of cell polarization in most eukaryotic cells is the conserved Rho GTPase, Cdc42. In budding yeast, Cdc42 is activatedbyasingleguaninenucleotideexchangefactor,Cdc24.ThemechanisticdetailsofCdc24activationattheonsetof yeastcellpolarizationareunclear.PreviousstudieshavesuggestedanimportantroleforphosphorylationofCdc24,which mayregulateactivityorfunctionoftheprotein,representingakeystepinthesymmetrybreakingprocess. Methodology/Principal Findings: Here, we directly ask whether multisite phosphorylation of Cdc24 plays a role in its regulation.Weidentifythroughmassspectrometryanalysisoverthirtyputativeinvivophosphorylationsites.Wefirstfocus onsitesmatchingconsensussequencesforcyclin-dependentandp21-activatedkinases,twokinasefamiliesthathavebeen previouslyshowntophosphorylateCdc24.Throughsite-directedmutagenesis,yeastgenetics,andlightandfluorescence microscopy, we show that nonphosphorylatable mutations of these consensus sites do not lead to any detectable consequencesongrowthrate,morphology,kineticsofpolarization,orlocalizationofthemutantprotein.Wedo,however, observeachangeinthemobilityshiftofmutantCdc24proteinsonSDS,suggestingthatwehaveindeedperturbed itsphosphorylation.Finally,weshowthatmutationofallidentifiedphosphorylationsitesdoesnotcauseobservabledefects ingrowthrateormorphology. Conclusions/Signific