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dc.contributor.authorSalewskij, Kirill
dc.contributor.authorRieger, Bettina
dc.contributor.authorHager, Frances
dc.contributor.authorArroum, Tasnim
dc.contributor.authorDuwe, Patrick
dc.contributor.authorVillalta, Jimmy
dc.contributor.authorColgiati, Sara
dc.contributor.authorRichter, Christian P
dc.contributor.authorPsathaki, Olympia E
dc.contributor.authorEnriquez, José Antonio 
dc.contributor.authorDellmann, Timo
dc.contributor.authorBusch, Karin B
dc.date.accessioned2020-09-22T13:29:26Z
dc.date.available2020-09-22T13:29:26Z
dc.date.issued2020-01
dc.identifier.citationBiochim Biophys Acta Bioenerg. 2020; 1861(1):148091es_ES
dc.identifier.urihttp://hdl.handle.net/20.500.12105/11071
dc.description.abstractF1FO ATP synthase, also known as complex V, is a key enzyme of mitochondrial energy metabolism that can synthesize and hydrolyze ATP. It is not known whether the ATP synthase and ATPase function are correlated with a different spatio-temporal organisation of the enzyme. In order to analyze this, we tracked and localized single ATP synthase molecules in situ using live cell microscopy. Under normal conditions, complex V was mainly restricted to cristae indicated by orthogonal trajectories along the cristae membranes. In addition confined trajectories that are quasi immobile exist. By inhibiting glycolysis with 2-DG, the activity and mobility of complex V was altered. The distinct cristae-related orthogonal trajectories of complex V were obliterated. Moreover, a mobile subpopulation of complex V was found in the inner boundary membrane. The observed changes in the ratio of dimeric/monomeric complex V, respectively less mobile/more mobile complex V and its activity changes were reversible. In IF1-KO cells, in which ATP hydrolysis is not inhibited by IF1, complex V was more mobile, while inhibition of ATP hydrolysis by BMS-199264 reduced the mobility of complex V. Taken together, these data support the existence of different subpopulations of complex V, ATP synthase and ATP hydrolase, the latter with higher mobility and probably not prevailing at the cristae edges. Obviously, complex V reacts quickly and reversibly to metabolic conditions, not only by functional, but also by spatial and structural reorganization.es_ES
dc.description.sponsorshipThis work was supported by the DFG (INST 190/167-2). K. Busch is associated with the CiM (Cells in Motion cluster, Munster).es_ES
dc.language.isoenges_ES
dc.publisherElsevieres_ES
dc.relation.isversionofPublisher's versiones_ES
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/*
dc.subject.meshAdenosine Triphosphate es_ES
dc.subject.meshHeLa Cells es_ES
dc.subject.meshHumans es_ES
dc.subject.meshMitochondria es_ES
dc.subject.meshMitochondrial Membranes es_ES
dc.subject.meshMitochondrial Proteins es_ES
dc.subject.meshMitochondrial Proton-Translocating ATPases es_ES
dc.subject.meshProton-Translocating ATPases es_ES
dc.titleThe spatio-temporal organization of mitochondrial F1FO ATP synthase in cristae depends on its activity mode.es_ES
dc.typeArtículoes_ES
dc.rights.licenseAttribution-NonCommercial-NoDerivatives 4.0 Internacional*
dc.identifier.pubmedID31669489es_ES
dc.format.volume1861es_ES
dc.format.number1es_ES
dc.format.page148091es_ES
dc.identifier.doi10.1016/j.bbabio.2019.148091es_ES
dc.contributor.funderDFG - German Research Foundation
dc.description.peerreviewedes_ES
dc.identifier.e-issn1879-2650es_ES
dc.relation.publisherversionhttps://doi.org/10.1016/j.bbabio.2019.148091es_ES
dc.identifier.journalBiochimica et biophysica acta. Bioenergeticses_ES
dc.repisalud.orgCNICCNIC::Grupos de investigación::Genética Funcional del Sistema de Fosforilación Oxidativaes_ES
dc.repisalud.institucionCNICes_ES
dc.rights.accessRightsinfo:eu-repo/semantics/openAccesses_ES


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Attribution-NonCommercial-NoDerivatives 4.0 Internacional
This item is licensed under a: Attribution-NonCommercial-NoDerivatives 4.0 Internacional