Restricted diffusion of OXPHOS complexes in dynamic mitochondria delays their exchange between cristae and engenders a transitory mosaic distribution

DC FieldValueLanguage
dc.contributor.authorWilkens, Verena
dc.contributor.authorKohl, Wladislaw
dc.contributor.authorBusch, Karin
dc.date.accessioned2021-12-23T16:02:39Z-
dc.date.available2021-12-23T16:02:39Z-
dc.date.issued2013
dc.identifier.issn00219533
dc.identifier.urihttps://osnascholar.ub.uni-osnabrueck.de/handle/unios/5538-
dc.description.abstractMitochondria are involved in cellular energy supply, signaling and apoptosis. Their ability to fuse and divide provides functional and morphological flexibility and is a key feature in mitochondrial quality maintenance. To study the impact of mitochondrial fusion/fission on the reorganization of inner membrane proteins, oxidative phosphorylation (OXPHOS) complexes in mitochondria of different HeLa cells were tagged with fluorescent proteins (GFP and DsRed-HA), and cells were fused by polyethylene glycol treatment. Redistribution of the tagged OXPHOS complexes was then followed by means of immunoelectron microscopy, two color super-resolution fluorescence microscopy and single molecule tracking. In contrast to outer membrane and matrix proteins, which mix quickly and homogeneously upon mitochondrial fusion, the mixing of inner membrane proteins was decelerated. Our data suggest that the composition of cristae is preserved during fusion of mitochondria and that cristae with mixed OXPHOS complexes are only slowly and successively formed by restricted diffusion of inner membrane proteins into existing cristae. The resulting transitory mosaic composition of the inner mitochondrial membrane illuminates mitochondrial heterogeneity and potentially is linked to local differences in function and membrane potential.
dc.description.sponsorshipDeutsche ForschungsgemeinschaftGerman Research Foundation (DFG) [Bu 2288/1]; [SFB 944]; The study was supported by the Deutsche Forschungsgemeinschaft [grant number Bu 2288/1 to K. B. B.] and a SFB 944 grant to K.B.B.
dc.language.isoen
dc.publisherCOMPANY BIOLOGISTS LTD
dc.relation.ispartofJOURNAL OF CELL SCIENCE
dc.subjectATP SYNTHASE
dc.subjectCell Biology
dc.subjectCELLS
dc.subjectCRYSTAL-STRUCTURE
dc.subjectFISSION
dc.subjectFUSION
dc.subjectImmunoelectron microscopy (IEM)
dc.subjectLOCALIZATION
dc.subjectMEMBRANE ORGANIZATION
dc.subjectMembrane protein diffusion
dc.subjectMitochondrial fusion and fission dynamics
dc.subjectMitochondrial microcompartments
dc.subjectOxidative phosphorylation
dc.subjectOXIDATIVE STRESS
dc.subjectSHAPE CHANGES
dc.subjectSuper-resolution tracking and localization microscopy
dc.subjectSUPERCOMPLEXES
dc.titleRestricted diffusion of OXPHOS complexes in dynamic mitochondria delays their exchange between cristae and engenders a transitory mosaic distribution
dc.typejournal article
dc.identifier.doi10.1242/jcs.108852
dc.identifier.isiISI:000316460800012
dc.description.volume126
dc.description.issue1
dc.description.startpage103
dc.description.endpage116
dc.contributor.orcid0000-0003-0525-0191
dc.contributor.researcheridABH-8594-2020
dc.contributor.researcheridAAM-8374-2021
dc.identifier.eissn14779137
dc.publisher.placeBIDDER BUILDING, STATION RD, HISTON, CAMBRIDGE CB24 9LF, ENGLAND
dcterms.isPartOf.abbreviationJ. Cell Sci.
dcterms.oaStatusBronze
crisitem.author.deptUniversität Osnabrück-
crisitem.author.deptFB 05 - Biologie/Chemie-
crisitem.author.deptidfb05-
crisitem.author.orcid0000-0003-0525-0191-
crisitem.author.parentorgUniversität Osnabrück-
crisitem.author.netidKoWl001-
crisitem.author.netidBuKa152-
Show simple item record

Page view(s)

2
Last Week
0
Last month
0
checked on Apr 14, 2024

Google ScholarTM

Check

Altmetric