Entropic Tension in Crowded Membranes 英文参考文献.docVIP

EntropicTensioninCrowdedMembranes MartinLinde′n1¤,PierreSens2,RobPhillips1,2,3* 1DepartmentofAppliedPhysics,CaliforniaInstituteofTechnology,Pasadena,California,UnitedStatesofAmerica,2LaboratoiredePhysico-ChimieThe′orique,CNRS/ UMR7083,ESPCI,Paris,France,3DivisionofBiology,CaliforniaInstituteofTechnology,Pasadena,California,UnitedStatesofAmerica Abstract Unliketheirmodelmembranecounterparts,biologicalmembranesarerichlydecoratedwithaheterogeneousassemblyof membrane proteins. These proteins are so tightly packed that their excluded area interactions can alter the free energy landscapecontrollingtheconformationaltransitionssufferedbysuchproteins.Formembranechannels,thiseffectcanalter thecriticalmembranetensionatwhichtheyundergoatransitionfromaclosedtoanopenstate,andthereforeinfluence proteinfunctioninvivo.Despitetheirobviousimportance,crowdingphenomenainmembranesaremuchlesswellstudied thaninthecytoplasm.Usingstatisticalmechanicsresultsforharddiskliquids,weshowthatcrowdinginducesanentropic tension in the membrane, which influences transitions that alter the projected area and circumference of a membrane protein.Asaspecificcasestudyinthiseffect, weconsidertheimpactofcrowdingonthegating propertiesofbacterial mechanosensitive membrane channels, which are thought to confer osmoprotection when these cells are subjected to osmotic shock. We find that crowding can alter the gating energies by more than 2kBT in physiological conditions, a substantialfractionofthetotalgatingenergiesinsomecases.Giventheubiquityofmembranecrowding,thenonspecific nature of excluded volume interactions, and the fact that the function of many membrane proteins involve significant conformationalchanges,thisspecificcasestudyhighlightsageneralaspectinthefunctionofmembraneproteins. Citation:Linde′n M,SensP,PhillipsR(2012)EntropicTensioninCrowdedMembranes.PLoSComputBiol8(3):e1002431.doi:10.1371/journal.pcbi.1002431 Editor:EmadTajkhorshid,UniversityofIllinois,UnitedStatesofAmerica ReceivedOctober1