APOOL Is a Cardiolipin-Binding Constituent of the MitofilinMINOS Protein Complex Determining Cristae Morphology in Mammalian Mitochondria.docVIP

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APOOL Is a Cardiolipin-Binding Constituent of the MitofilinMINOS Protein Complex Determining Cristae Morphology in Mammalian Mitochondria.doc

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APOOL Is a Cardiolipin-Binding Constituent of the MitofilinMINOS Protein Complex Determining Cristae Morphology in Mammalian Mitochondria

APOOLIsaCardiolipin-BindingConstituentofthe Mitofilin/MINOSProteinComplexDeterminingCristae MorphologyinMammalianMitochondria TobiasA.Weber1,2,SebastianKoob1,2,HeinrichHeide3,IlkaWittig3,BrianHead4, AlexandervanderBliek4,UlrichBrandt3,MichelMittelbronn5,AndreasS.Reichert1,2* 1Mitochondrial Biology, Buchmann Institute for Molecular Life Sciences, Goethe University, Frankfurt am Main, Germany, 2Mitochondriale Biologie, Zentrum fu¨r MolekulareMedizin,GoetheUniversita¨t, FrankfurtamMain,Germany,3MolecularBioenergeticsGroup,MedicalSchool,ClusterofExcellenceFrankfurtMacromolecular Complexes,GoetheUniversity,FrankfurtamMain,Germany,4DepartmentofBiologicalChemistry,DavidGeffenSchoolofMedicine,UniversityofCaliforniaLosAngeles, LosAngeles,California,UnitedStatesofAmerica,5InstituteofNeurology,EdingerInstitute,GoetheUniversity,FrankfurtamMain,Germany Abstract Mitochondrial cristae morphology is highly variable and altered under numerous pathological conditions. The protein complexes involved are largely unknown or only insufficiently characterized. Using complexome profiling we identified apolipoproteinO(APOO)andapolipoproteinO-likeprotein(APOOL)asputativecomponentsoftheMitofilin/MINOSprotein complex which was recently implicated in determining cristae morphology. We show that APOOL is a mitochondrial membraneproteinfacingtheintermembranespace.Itspecificallybindstocardiolipininvitrobutnottotheprecursorlipid phosphatidylglycerol. Overexpression of APOOL led to fragmentation of mitochondria, a reduced basal oxygen consumption rate, and altered cristae morphology. Downregulation of APOOL impaired mitochondrial respiration and causedmajoralterationsincristaemorphology.WefurthershowthatAPOOLphysicallyinteractswithseveralsubunitsof theMINOScomplex,namelyMitofilin,MINOS1,andSAMM50.WeconcludethatAPOOLisacardiolipin-bindingcomponent oftheMitofilin/MINOSproteincomplexdeterminingcristaemorphologyinmammalianmitochondria.Ourfindingsfurther assignanintracellularroletoamemberoftheapolip