Evidence map›Paper›PMID 37278158›Full record

ArticleEMBO reports2023

Human mitochondrial ADP/ATP carrier SLC25A4 operates with a ping-pong kinetic mechanism.

Camila Cimadamore-Werthein, Stephany Jaiquel Baron, Martin S King, Roger Springett, Edmund Rs Kunji

Open access · hybridAbstract read
In one paragraph

Article in EMBO reports, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
4.6field-weighted citation impact, top 5% 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

28 citing papers in PubMed, 30 citations in OpenAlex.

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  15. A genome-wide association study identified 10 novel genomic loci associated with intrinsic capacity.The journals of gerontology. Series A, Biological sciences and medical sciences · 2025
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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

5 authors at 2 institutions in 1 country.

Camila Cimadamore-Werthein *Medical Research Council Mitochondrial Biology Unit, The Keith Peters Building, Cambridge Biomedical Campus, Cambridge, UK.ORCID 0000-0001-5507-817X
Stephany Jaiquel Baron *Medical Research Council Mitochondrial Biology Unit, The Keith Peters Building, Cambridge Biomedical Campus, Cambridge, UK.
Martin S KingMedical Research Council Mitochondrial Biology Unit, The Keith Peters Building, Cambridge Biomedical Campus, Cambridge, UK.ORCID 0000-0001-6030-5154
Roger SpringettCellSpex, Kettering, Northamptonshire, UK.
Edmund Rs KunjiMedical Research Council Mitochondrial Biology Unit, The Keith Peters Building, Cambridge Biomedical Campus, Cambridge, UK.ORCID 0000-0002-0610-4500
MRC Mitochondrial Biology Unit · GBNorthamptonshire Healthcare NHS Foundation Trust · GB

Funding

Biotechnology and Biological Sciences Research CouncilMedical Research Council MC_UU_00028/2
6 · The paper itself

Abstract

The mitochondrial ADP/ATP carrier (SLC25A4), also called the adenine nucleotide translocase, imports ADP into the mitochondrial matrix and exports ATP, which are key steps in oxidative phosphorylation. Historically, the carrier was thought to form a homodimer and to operate by a sequential kinetic mechanism, which involves the formation of a ternary complex with the two exchanged substrates bound simultaneously. However, recent structural and functional data have demonstrated that the mitochondrial ADP/ATP carrier works as a monomer and has a single substrate binding site, which cannot be reconciled with a sequential kinetic mechanism. Here, we study the kinetic properties of the human mitochondrial ADP/ATP carrier by using proteoliposomes and transport robotics. We show that the Km/Vmax ratio is constant for all of the measured internal concentrations. Thus, in contrast to earlier claims, we conclude that the carrier operates with a ping-pong kinetic mechanism in which substrate exchange across the membrane occurs consecutively rather than simultaneously. These data unite the kinetic and structural models, showing that the carrier operates with an alternating access mechanism.

Indexed as

MitochondriaMitochondrial ADP, ATP TranslocasesAdenine Nucleotide Translocator 1Adenosine DiphosphateAdenosine TriphosphateHumansKineticsAdenine Nucleotide Translocator 1Adenosine DiphosphateAdenosine TriphosphateMitochondrial ADP, ATP TranslocasesSLC25A4 protein, humanadenine nucleotide translocatorADP/ATP translocasebioenergeticsmitochondrial carrier familySLC25

Identifiers

PMID37278158
PMCPMC10398649
OpenAlexW4379508928

What OpenQuestion holds

Textmetadata
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.