The mitochondrial chaperone TRAP1 regulates F-ATP synthase channel formation.
Humans
Mitochondrial Permeability Transition Pore
/ metabolism
Mitochondrial Membrane Transport Proteins
/ metabolism
Mitochondrial Proton-Translocating ATPases
/ metabolism
Peptidyl-Prolyl Isomerase F
/ metabolism
Mitochondria
/ metabolism
Molecular Chaperones
/ metabolism
Adenosine Triphosphate
/ metabolism
HSP90 Heat-Shock Proteins
/ metabolism
Journal
Cell death and differentiation
ISSN: 1476-5403
Titre abrégé: Cell Death Differ
Pays: England
ID NLM: 9437445
Informations de publication
Date de publication:
12 2022
12 2022
Historique:
received:
20
02
2022
accepted:
12
05
2022
revised:
11
05
2022
pubmed:
26
5
2022
medline:
17
12
2022
entrez:
25
5
2022
Statut:
ppublish
Résumé
Binding of the mitochondrial chaperone TRAP1 to client proteins shapes bioenergetic and proteostatic adaptations of cells, but the panel of TRAP1 clients is only partially defined. Here we show that TRAP1 interacts with F-ATP synthase, the protein complex that provides most cellular ATP. TRAP1 competes with the peptidyl-prolyl cis-trans isomerase cyclophilin D (CyPD) for binding to the oligomycin sensitivity-conferring protein (OSCP) subunit of F-ATP synthase, increasing its catalytic activity and counteracting the inhibitory effect of CyPD. Electrophysiological measurements indicate that TRAP1 directly inhibits a channel activity of purified F-ATP synthase endowed with the features of the permeability transition pore (PTP) and that it reverses PTP induction by CyPD, antagonizing PTP-dependent mitochondrial depolarization and cell death. Conversely, CyPD outcompetes the TRAP1 inhibitory effect on the channel. Our data identify TRAP1 as an F-ATP synthase regulator that can influence cell bioenergetics and survival and can be targeted in pathological conditions where these processes are dysregulated, such as cancer.
Identifiants
pubmed: 35614131
doi: 10.1038/s41418-022-01020-0
pii: 10.1038/s41418-022-01020-0
pmc: PMC9751095
doi:
Substances chimiques
Mitochondrial Permeability Transition Pore
0
Mitochondrial Membrane Transport Proteins
0
Mitochondrial Proton-Translocating ATPases
EC 3.6.3.-
Peptidyl-Prolyl Isomerase F
0
Molecular Chaperones
0
Adenosine Triphosphate
8L70Q75FXE
TRAP1 protein, human
0
HSP90 Heat-Shock Proteins
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
2335-2346Informations de copyright
© 2022. The Author(s).
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