The f subunit of human ATP synthase is essential for normal mitochondrial morphology and permeability transition.
ATP synthase
f subunit
mitochondrial morphology
permeability transition pore, PTP
Journal
Cell reports
ISSN: 2211-1247
Titre abrégé: Cell Rep
Pays: United States
ID NLM: 101573691
Informations de publication
Date de publication:
11 05 2021
11 05 2021
Historique:
received:
24
02
2020
revised:
11
03
2021
accepted:
20
04
2021
entrez:
12
5
2021
pubmed:
13
5
2021
medline:
10
2
2022
Statut:
ppublish
Résumé
The f subunit is localized at the base of the ATP synthase peripheral stalk. Its function in the human enzyme is poorly characterized. Because full disruption of its ATP5J2 gene with the CRISPR-Cas9 strategy in the HAP1 human model has been shown to cause alterations in the amounts of other ATP synthase subunits, here we investigated the role of the f subunit in HeLa cells by regulating its levels through RNA interference. We confirm the role of the f subunit in ATP synthase dimer stability and observe that its downregulation per se does not alter the amounts of the other enzyme subunits or ATP synthase synthetic/hydrolytic activity. We show that downregulation of the f subunit causes abnormal crista organization and decreases permeability transition pore (PTP) size, whereas its re-expression in f subunit knockdown cells rescues mitochondrial morphology and PTP-dependent swelling.
Identifiants
pubmed: 33979610
pii: S2211-1247(21)00445-9
doi: 10.1016/j.celrep.2021.109111
pii:
doi:
Substances chimiques
Mitochondrial Proton-Translocating ATPases
EC 3.6.3.-
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
109111Informations de copyright
Copyright © 2021 The Authors. Published by Elsevier Inc. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of interests The authors declare no competing interests.