Evidence map›Paper›PMID 35614131›Full record

ArticleCell death and differentiation2022

The mitochondrial chaperone TRAP1 regulates F-ATP synthase channel formation.

Giuseppe Cannino, Andrea Urbani, Marco Gaspari, Mariaconcetta Varano, Alessandro Negro, Antonio Filippi, Francesco Ciscato, Ionica Masgras, Christoph Gerle, Elena Tibaldi and 5 more

Open access · hybridAbstract read
In one paragraph

Article in Cell death and differentiation, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
3.5field-weighted citation impact, top 6% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

29 citing papers in PubMed, 41 citations in OpenAlex.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

15 authors at 5 institutions in 2 countries.

Giuseppe CanninoDepartment of Biomedical Sciences, University of Padova, via U. Bassi 58/B, 35131, Padova, Italy.
Andrea UrbaniDepartment of Biomedical Sciences, University of Padova, via U. Bassi 58/B, 35131, Padova, Italy.
Marco GaspariResearch Centre for Advanced Biochemistry and Molecular Biology, Department of Experimental and Clinical Medicine, Magna Graecia University of Catanzaro, viale Europa, 88100, Catanzaro, Italy.
Mariaconcetta VaranoResearch Centre for Advanced Biochemistry and Molecular Biology, Department of Experimental and Clinical Medicine, Magna Graecia University of Catanzaro, viale Europa, 88100, Catanzaro, Italy.
Alessandro NegroDepartment of Biomedical Sciences, University of Padova, via U. Bassi 58/B, 35131, Padova, Italy.ORCID 0000-0003-3142-7632
Antonio FilippiDepartment of Medicine, University of Udine, via Colugna 50, 33100, Udine, Italy.
Francesco CiscatoDepartment of Biomedical Sciences, University of Padova, via U. Bassi 58/B, 35131, Padova, Italy.
Ionica MasgrasDepartment of Biomedical Sciences, University of Padova, via U. Bassi 58/B, 35131, Padova, Italy.
Christoph GerleInstitute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka, Japan.
Elena TibaldiDepartment of Molecular Medicine, University of Padova, via Gabelli 63, 35121, Padova, Italy.
Anna Maria BrunatiDepartment of Molecular Medicine, University of Padova, via Gabelli 63, 35121, Padova, Italy.
Giorgio ColomboDepartment of Chemistry, University of Pavia, via Taramelli 12, 27100, Pavia, Italy.
Giovanna LippeDepartment of Medicine, University of Udine, via Colugna 50, 33100, Udine, Italy.
Paolo BernardiDepartment of Biomedical Sciences, University of Padova, via U. Bassi 58/B, 35131, Padova, Italy.ORCID 0000-0001-9187-3736
Andrea RasolaDepartment of Biomedical Sciences, University of Padova, via U. Bassi 58/B, 35131, Padova, Italy. andrea.rasola@unipd.it.ORCID 0000-0003-4522-3008
University of Padua · ITMagna Graecia University · ITUniversity of Udine · ITSPring-8 · JPUniversity of Pavia · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

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.

Indexed as

Mitochondrial Membrane Transport ProteinsMitochondrial Permeability Transition PoreAdenosine TriphosphateHSP90 Heat-Shock ProteinsHumansMitochondriaMitochondrial Proton-Translocating ATPasesMolecular ChaperonesPeptidyl-Prolyl Isomerase FAdenosine TriphosphateHSP90 Heat-Shock ProteinsMitochondrial Membrane Transport ProteinsMitochondrial Permeability Transition PoreMitochondrial Proton-Translocating ATPasesMolecular ChaperonesPeptidyl-Prolyl Isomerase FTRAP1 protein, human

Identifiers

PMID35614131
PMCPMC9751095
OpenAlexW4281483656

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.