Defining the molecular mechanisms of the mitochondrial permeability transition through genetic manipulation of F-ATP synthase.
Calcium
/ metabolism
Carbonyl Cyanide p-Trifluoromethoxyphenylhydrazone
/ pharmacology
Cell Line, Tumor
HeLa Cells
Humans
Membrane Potential, Mitochondrial
/ drug effects
Mitochondria
/ drug effects
Mitochondrial Permeability Transition Pore
/ metabolism
Mitochondrial Proton-Translocating ATPases
/ genetics
Protein Subunits
/ genetics
Proton Ionophores
/ pharmacology
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
10 08 2021
10 08 2021
Historique:
received:
03
05
2021
accepted:
26
07
2021
entrez:
11
8
2021
pubmed:
12
8
2021
medline:
24
8
2021
Statut:
epublish
Résumé
F-ATP synthase is a leading candidate as the mitochondrial permeability transition pore (PTP) but the mechanism(s) leading to channel formation remain undefined. Here, to shed light on the structural requirements for PTP formation, we test cells ablated for g, OSCP and b subunits, and ρ
Identifiants
pubmed: 34376679
doi: 10.1038/s41467-021-25161-x
pii: 10.1038/s41467-021-25161-x
pmc: PMC8355262
doi:
Substances chimiques
Mitochondrial Permeability Transition Pore
0
Protein Subunits
0
Proton Ionophores
0
Carbonyl Cyanide p-Trifluoromethoxyphenylhydrazone
370-86-5
Mitochondrial Proton-Translocating ATPases
EC 3.6.3.-
Calcium
SY7Q814VUP
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
4835Informations de copyright
© 2021. The Author(s).
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