Protein Scaffolds Can Enhance the Bistability of Multisite Phosphorylation Systems 英文参考文献.docVIP

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Protein Scaffolds Can Enhance the Bistability of Multisite Phosphorylation Systems 英文参考文献.doc

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Protein Scaffolds Can Enhance the Bistability of Multisite Phosphorylation Systems 英文参考文献

ProteinScaffoldsCanEnhancetheBistabilityofMultisite PhosphorylationSystems CarloChan1,XinfengLiu2,LimingWang3,LeeBardwell4,QingNie1.,Germa′nEnciso1. * 1DepartmentofMathematics,CenterforMathematicalandComplexBiologicalSystems,CenterforComplexBiologicalSystems,UniversityofCalifornia,Irvine,California, UnitedStatesofAmerica,2DepartmentofMathematics,UniversityofSouthCarolina,Columbia,SouthCarolina,UnitedStatesofAmerica,3DepartmentofMathematics, CaliforniaStateUniversity,LosAngeles,California,UnitedStatesofAmerica,4DepartmentofDevelopmentalandCellBiology,SchoolofBiologicalSciences,Universityof California,Irvine,California,UnitedStatesofAmerica Abstract The phosphorylation of a substrate at multiple sites is a common protein modification that can give rise to important structuralandelectrostaticchanges.Scaffoldproteinscanenhanceproteinphosphorylationbyfacilitatinganinteraction between a protein kinase enzyme and its target substrate. In this work we consider a simple mathematical model of a scaffoldproteinandshowthatunderspecificconditions,thepresenceofthescaffoldcansubstantiallyraisethelikelihood thattheresulting systemwill exhibitbistable behavior. Thisphenomenonis especiallypronounced when theenzymatic reactionshavesufficientlylargeKM,comparedtotheconcentrationofthetargetsubstrate.Wealsofindforacloselyrelated modelthatbistablesystemstendtohaveaspecifickineticconformation.Usingdeficiencytheoryandothermethods,we provideanumberofnecessaryconditionsforbistability,suchasthepresenceofmultiplephosphorylationsitesandthe dependenceofthescaffoldbinding/unbindingratesonthenumberofphosphorylatedsites. Citation:ChanC,LiuX,WangL,BardwellL,NieQ,etal.(2012)ProteinScaffoldsCanEnhancetheBistabilityofMultisitePhosphorylationSystems.PLoSComput Biol8(6):e1002551.doi:10.1371/journal.pcbi.1002551 Editor:JorgStelling,ETHZurich,Switzerland ReceivedJune16,2011;AcceptedApril23,2012;PublishedJune21,2012 Copyright: ? 2012 Chan et al. This is an open-access article distributed under the terms o