Quantitative Mass Spectrometry Analysis Reveals Similar Substrate Consensus Motif for Human Mps1 Kinase and Plk1 英文参考文献.docVIP

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Quantitative Mass Spectrometry Analysis Reveals Similar Substrate Consensus Motif for Human Mps1 Kinase and Plk1 英文参考文献.doc

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Quantitative Mass Spectrometry Analysis Reveals Similar Substrate Consensus Motif for Human Mps1 Kinase and Plk1 英文参考文献

QuantitativeMassSpectrometryAnalysisRevealsSimilar SubstrateConsensusMotifforHumanMps1Kinaseand Plk1 ZhenDou1,3*.,ConradvonSchubert2.,RomanKo¨rner1¤a,AnnaSantamaria1,2,SabineElowe1¤b,ErichA. Nigg1,2 * 1DepartmentofCellBiology,MaxPlanckInstituteofBiochemistry,Martinsried,Germany,2Biozentrum,UniversityofBasel,Basel,Switzerland,3HefeiNationalLaboratory ofPhysicalSciencesattheMicroscale,UniversityofScienceandTechnologyofChina,Hefei,China Abstract Background:MembersoftheMps1kinasefamilyplayanessentialandevolutionarilyconservedroleinthespindleassembly checkpoint(SAC),asurveillancemechanismthatensuresaccuratechromosomesegregationduringmitosis.HumanMps1 (hMps1) is highly phosphorylated during mitosis and many phosphorylation sites have been identified. However, the upstreamkinasesresponsibleforthesephosphorylationsarenotpresentlyknown. Methodology/Principal Findings: Here, we identify 29 in vivo phosphorylation sites in hMps1. While in vivo analyses indicatethatAuroraBandhMps1activityarerequiredformitotichyper-phosphorylationofhMps1,invitrokinaseassays showthatCdk1,MAPK,Plk1andhMps1itselfcandirectlyphosphorylatehMps1.AlthoughAuroraBpoorlyphosphorylates hMps1invitro,itpositivelyregulatesthelocalizationofMps1tokinetochoresinvivo.Mostimportantly,quantitativemass spectrometry analysis demonstrates that at least 12 sites within hMps1 can be attributed to autophosphorylation. Remarkably,thesehMps1autophosphorylationsitescloselyresembletheconsensusmotifofPlk1,demonstratingthatthese twomitotickinasesshareasimilarsubstrateconsensus. Conclusions/Significance:hMps1kinaseisregulatedbyAuroraBkinaseanditsautophosphorylation.AnalysisonhMps1 autophosphorylationsitesdemonstratesthathMps1hasasubstratepreferencesimilartoPlk1kinase. Citation:DouZ,vonSchubertC,Ko¨rnerR,SantamariaA,EloweS,etal.(2011)QuantitativeMassSpectrometryAnalysisRevealsSimilarSubstrateConsensus MotifforHumanMps1KinaseandPlk1.PLoSONE6(4):e18793.doi:10.1371/journal.pone.0018793 Editor:ZiyinLi,UniversityofTexas-HoustonMedi