Rho Kinases Role in Myosin Recruitment to the Equatorial Cortex of Mitotic Drosophila S2 Cells Is for Myosin Regulatory Light Chain Phosphorylation 英文参考文献.docVIP

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Rho Kinases Role in Myosin Recruitment to the Equatorial Cortex of Mitotic Drosophila S2 Cells Is for Myosin Regulatory Light Chain Phosphorylation 英文参考文献.doc

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Rho Kinases Role in Myosin Recruitment to the Equatorial Cortex of Mitotic Drosophila S2 Cells Is for Myosin Regulatory Light Chain Phosphorylation 英文参考文献

RhoKinase’sRoleinMyosinRecruitmenttothe EquatorialCortexofMitoticDrosophilaS2CellsIsfor MyosinRegulatoryLightChainPhosphorylation SaraO.Dean,JamesA.Spudich* DepartmentofBiochemistry,StanfordUniversity,Stanford,California,UnitedStatesofAmerica Background.MyosinIIrecruitmenttotheequatorialcortexisoneoftheearliesteventsinestablishmentofthecytokinetic contractilering.InDrosophilaS2cells,wepreviouslyshowedthatmyosinIIisrecruitedtothefurrowindependentlyofF-actin, andthatRho1andRokareessentialforthisrecruitment[1].Rokphosphorylatesseveralcellularproteins,includingthemyosin regulatorylightchain(RLC).Methodology/PrincipalFindings.Hereweexpressphosphorylationstatemimicconstructsof theRLCinS2cellstoexaminetheroleofRLCphosphorylationinvolvingRokinthelocalizationofmyosin.Phosphorylationof the RLC is required for myosin localization to the equatorial cortex during mitosis, and the essential role of Rok in this localizationandforcytokinesisistomaintainphosphorylationoftheRLC.TheabilitytoregulatetheRLCphosphorylationstate spatio-temporally is not essential for the myosin localization. Furthermore, the essential role of Citron in cytokinesis is not phosphorylationoftheRLC.Conclusions/Significance.WeconcludethattheRho1pathwayleadingtomyosinlocalizationto the future cytokinetic furrow is relatively straightforward, where only Rok is needed, and it is only needed to maintain phosphorylationofthemyosinRLC. Citation: DeanSO,SpudichJA(2006)RhoKinase’sRoleinMyosinRecruitmenttotheEquatorialCortexofMitoticDrosophilaS2CellsIsforMyosin RegulatoryLightChainPhosphorylation.PLoSONE1(1):e131.doi:10.1371/journal.pone.0000131 INTRODUCTION Drosophila embryos in mutants of CP190, a protein that interacts withcentrosomesduringmitosisandbindstomicrotubulesinvitro [17]. However, Jordan and Karess reported that non-phosphor- ylatableRLCiscorrectlylocalizedinDrosophilaeggchambers[9], suggestingthatdifferentcellulareventsinvolvingmyosinIImaybe regulated differently. Thus, we wanted to test specifically fo