Autoinactivation of the Stargazin–AMPA Receptor Complex Subunit-Dependency and Independence from Physical Dissociation 英文参考文献.docVIP

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Autoinactivation of the Stargazin–AMPA Receptor Complex Subunit-Dependency and Independence from Physical Dissociation 英文参考文献.doc

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Autoinactivation of the Stargazin–AMPA Receptor Complex Subunit-Dependency and Independence from Physical Dissociation 英文参考文献

AutoinactivationoftheStargazin–AMPAReceptor Complex:Subunit-DependencyandIndependencefrom PhysicalDissociation ArturSemenov1,TommiMo¨ykkynen1,2,SarahK.Coleman1,EsaR.Korpi2,KariKeina¨nen1* 1DepartmentofBiosciences,DivisionofBiochemistryandBiotechnology,UniversityofHelsinki,Helsinki,Finland,2InstituteofBiomedicine,Pharmacology,Universityof Helsinki,Helsinki,Finland Abstract Agonistresponsesandchannelkineticsofnativea-amino-3-hydroxy-5-methyl-4-isoxazolepropionicacid(AMPA)receptors are modulated by transmembrane accessory proteins. Stargazin, the prototypical accessory protein, decreases desensitizationandincreasesagonist potencyatAMPAreceptors. Furthermore, inthepresenceofstargazin,thesteady- stateresponsesofAMPAreceptorsshowagradualdeclineathigherglutamateconcentrations.This‘‘autoinactivation’’has been assigned to physical dissociation of the stargazin-AMPA receptor complex and suggested to serve as a protective mechanism against overactivation. Here, we analyzed autoinactivation of GluA1–A4 AMPA receptors (all flip isoform) expressed in the presence of stargazin. Homomeric GluA1, GluA3, and GluA4 channels showed pronounced autoinactivation indicated by the bell-shaped steady-state dose response curves for glutamate. In contrast, homomeric GluA2i channels did not show significant autoinactivation. The resistance of GluA2 to autoinactivation showed striking dependence on the splice form as GluA2-flop receptors displayed clear autoinactivation. Interestingly, the resistance of GluA2-flipcontainingreceptorstoautoinactivationwastransferredontoheteromericreceptorsinadominantfashion.To examine the relationship of autoinactivation tophysical separation of stargazin from the AMPA receptor, we analyzed a GluA4-stargazin fusion protein. Notably, the covalently linked complex and separately expressed proteins expressed a similar level of autoinactivation. We conclude that autoinactivation is a subunit and splice form dependent property of AMPAreceptor-stargazincomple