Human mitochondrial uncoupling protein 3 functions as a metabolite transporter

Author:

De Leonardis Francesco1ORCID,Ahmed Amer1,Vozza Angelo1,Capobianco Loredana2,Riley Christopher L.3,Barile Simona Nicole1,Di Molfetta Daria1,Tiziani Stefano3,DiGiovanni John4,Palmieri Luigi1,Dolce Vincenza5ORCID,Fiermonte Giuseppe1ORCID

Affiliation:

1. Department of Bioscience, Biotechnology and Environment University of Bari Italy

2. Department of Biological and Environmental Sciences and Technologies University of Salento Lecce Italy

3. Department of Nutritional Sciences The University of Texas at Austin TX USA

4. Division of Pharmacology and Toxicology, College of Pharmacy The University of Texas at Austin TX USA

5. Department of Pharmacy, Health and Nutritional Sciences University of Calabria Rende Italy

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.

Funder

National Institutes of Health

Publisher

Wiley

Subject

Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics

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