Loss of respiratory complex I subunit NDUFB10 affects complex I assembly and supercomplex formation
DC Element | Wert | Sprache |
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dc.contributor.author | Arroum, Tasnim | |
dc.contributor.author | Borowski, Marie-Theres | |
dc.contributor.author | Marx, Nico | |
dc.contributor.author | Schmelter, Frank | |
dc.contributor.author | Scholz, Martin | |
dc.contributor.author | Psathaki, Olympia Ekaterini | |
dc.contributor.author | Hippler, Michael | |
dc.contributor.author | Enriquez, Jose Antonio | |
dc.contributor.author | Busch, Karin B. | |
dc.date.accessioned | 2023-07-12T06:56:25Z | - |
dc.date.available | 2023-07-12T06:56:25Z | - |
dc.date.issued | 2023 | |
dc.identifier.issn | 1431-6730 | |
dc.identifier.uri | http://osnascholar.ub.uni-osnabrueck.de/handle/unios/71935 | - |
dc.description.abstract | The orchestrated activity of the mitochondrial respiratory or electron transport chain (ETC) and ATP synthase convert reduction power (NADH, FADH(2)) into ATP, the cell's energy currency in a process named oxidative phosphorylation (OXPHOS). Three out of the four ETC complexes are found in supramolecular assemblies: complex I, III, and IV form the respiratory supercomplexes (SC). The plasticity model suggests that SC formation is a form of adaptation to changing conditions such as energy supply, redox state, and stress. Complex I, the NADH-dehydrogenase, is part of the largest supercomplex (CI CIII2 CIVn). Here, we demonstrate the role of NDUFB10, a subunit of the membrane arm of complex I, in complex I and supercomplex assembly on the one hand and bioenergetics function on the other. NDUFB10 knockout was correlated with a decrease of SCAF1, a supercomplex assembly factor, and a reduction of respiration and mitochondrial membrane potential. This likely is due to loss of proton pumping since the CI P- P -module is downregulated and the P- D -module is completely abolished in NDUFB10 knock outs. | |
dc.description.sponsorship | CRC944 [INST190/1672]; HFSP doctoral fellowship [RGP0016/2018]; CRC944 (the z-project); The study was supported by a grant from CRC944 (INST190/1672 and the z-project). Tasnim Arroum was supported by an HFSP doctoral fellowship (RGP0016/2018). | |
dc.language.iso | en | |
dc.publisher | WALTER DE GRUYTER GMBH | |
dc.relation.ispartof | BIOLOGICAL CHEMISTRY | |
dc.subject | ARCHITECTURE | |
dc.subject | Biochemistry & Molecular Biology | |
dc.subject | complex I | |
dc.subject | MITOCHONDRIA | |
dc.subject | NDUFB10 | |
dc.subject | OXPHOS | |
dc.subject | respiratory chain supercomplexes | |
dc.title | Loss of respiratory complex I subunit NDUFB10 affects complex I assembly and supercomplex formation | |
dc.type | journal article | |
dc.identifier.doi | 10.1515/hsz-2022-0309 | |
dc.identifier.isi | ISI:000957593500001 | |
dc.description.volume | 404 | |
dc.description.issue | 5 | |
dc.description.startpage | 399 | |
dc.description.endpage | 415 | |
dc.contributor.orcid | http://orcid.org/0000-0002-3671-2961 | |
dc.contributor.orcid | http://orcid.org/0009-0004-9644-3494 | |
dc.contributor.researcherid | M-8468-2016 | |
dc.identifier.eissn | 1437-4315 | |
dc.publisher.place | GENTHINER STRASSE 13, D-10785 BERLIN, GERMANY | |
dcterms.isPartOf.abbreviation | Biol. Chem. | |
dcterms.oaStatus | hybrid | |
local.import.remains | affiliations : University of Munster; University of Munster; University of Munster; University Osnabruck; Centro Nacional de Investigaciones Cardiovasculares (CNIC) | |
local.import.remains | earlyaccessdate : MAR 2023 | |
local.import.remains | web-of-science-index : Science Citation Index Expanded (SCI-EXPANDED) | |
crisitem.author.dept | FB 05 - Biologie/Chemie | - |
crisitem.author.deptid | fb05 | - |
crisitem.author.orcid | 0000-0002-4035-6840 | - |
crisitem.author.parentorg | Universität Osnabrück | - |
crisitem.author.netid | PsOl764 | - |
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geprüft am 08.06.2024