Evidence map›Paper›PMID 38058167›Full record

ArticleFEBS letters2024

Human mitochondrial uncoupling protein 3 functions as a metabolite transporter.

Francesco De Leonardis, Amer Ahmed, Angelo Vozza, Loredana Capobianco, Christopher L Riley, Simona Nicole Barile, Daria Di Molfetta, Stefano Tiziani, John DiGiovanni, Luigi Palmieri and 2 more

Open access · bronzeAbstract read
In one paragraph

Article in FEBS letters, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
2.1field-weighted citation impact, top 12% 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

12 citing papers in PubMed, 12 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

12 authors at 5 institutions in 2 countries.

Francesco De LeonardisDepartment of Bioscience, Biotechnology and Environment, University of Bari, Italy.ORCID 0000-0002-6278-1565
Amer AhmedDepartment of Bioscience, Biotechnology and Environment, University of Bari, Italy.
Angelo VozzaDepartment of Bioscience, Biotechnology and Environment, University of Bari, Italy.
Loredana CapobiancoDepartment of Biological and Environmental Sciences and Technologies, University of Salento, Lecce, Italy.
Christopher L RileyDepartment of Nutritional Sciences, The University of Texas at Austin, TX, USA.
Simona Nicole BarileDepartment of Bioscience, Biotechnology and Environment, University of Bari, Italy.
Daria Di MolfettaDepartment of Bioscience, Biotechnology and Environment, University of Bari, Italy.
Stefano TizianiDepartment of Nutritional Sciences, The University of Texas at Austin, TX, USA.
John DiGiovanniDivision of Pharmacology and Toxicology, College of Pharmacy, The University of Texas at Austin, TX, USA.
Luigi PalmieriDepartment of Bioscience, Biotechnology and Environment, University of Bari, Italy.
Vincenza DolceDepartment of Pharmacy, Health and Nutritional Sciences, University of Calabria, Rende, Italy.ORCID 0000-0003-2966-4866
Giuseppe FiermonteDepartment of Bioscience, Biotechnology and Environment, University of Bari, Italy.ORCID 0000-0002-6764-9395
University of Bari Aldo Moro · ITThe University of Texas at Austin · USAustin College · USUniversity of Calabria · ITUniversity of Salento · IT

Funding

Molecular mechanisms of thermogenesisR01DK089224 · NIDDK · UNIVERSITY OF TEXAS AT AUSTIN · PI DIGIOVANNI, JOHN · 2011 to 2023
$3.4M
NIDDK NIH HHS R01 DK089224NIH HHS R01DK089224
6 · The paper itself

Abstract

Since its discovery, a major debate about mitochondrial uncoupling protein 3 (UCP3) has been whether its metabolic actions result primarily from mitochondrial inner membrane proton transport, a process that decreases respiratory efficiency and ATP synthesis. However, UCP3 expression and activity are induced by conditions that would seem at odds with inefficient 'uncoupled' respiration, including fasting and exercise. Here, we demonstrate that the bacterially expressed human UCP3, reconstituted into liposomes, catalyses a strict exchange of aspartate, malate, sulphate and phosphate. The R282Q mutation abolishes the transport activity of the protein. Although the substrate specificity and inhibitor sensitivity of UCP3 display similarity with that of its close homolog UCP2, the two proteins significantly differ in their transport mode and kinetic constants.

Indexed as

Ion ChannelsMitochondrial ProteinsHumansUncoupling Protein 1Uncoupling Protein 2Uncoupling Protein 3Ion ChannelsMitochondrial ProteinsUCP3 protein, humanUncoupling Protein 1Uncoupling Protein 2Uncoupling Protein 3amino acid transportanion transportbioenergeticsmitochondrial metabolismmitochondrial transportuncoupling protein

Identifiers

PMID38058167
PMCPMC10922436
OpenAlexW4389425770

What OpenQuestion holds

Textmetadata
LicenceTDM
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.