Sie können Bookmarks mittels Listen verwalten, loggen Sie sich dafür bitte in Ihr SLUB Benutzerkonto ein.
Medientyp:
E-Artikel
Titel:
Human mitochondrial uncoupling protein 3 functions as a metabolite transporter
Beteiligte:
De Leonardis, Francesco;
Ahmed, Amer;
Vozza, Angelo;
Capobianco, Loredana;
Riley, Christopher L.;
Barile, Simona Nicole;
Di Molfetta, Daria;
Tiziani, Stefano;
DiGiovanni, John;
Palmieri, Luigi;
Dolce, Vincenza;
Fiermonte, Giuseppe
Erschienen:
Wiley, 2024
Erschienen in:
FEBS Letters, 598 (2024) 3, Seite 338-346
Sprache:
Englisch
DOI:
10.1002/1873-3468.14784
ISSN:
0014-5793;
1873-3468
Entstehung:
Anmerkungen:
Beschreibung:
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.