Synergy of uncoupling proteins (1 and 2) with mitochondrial Ca uptake machinery potentiate mitochondrial uncoupling.

Furkan E Oflaz, Zhanat Koshenov, Martin Hirtl, Olaf A Bachkoenig, Wolfgang F Graier, Benjamin Gottschalk

Journal: Cell calcium 2023;112():102736

PMID: 37031662

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Abstract

Mitochondrial uncoupling proteins UCP1 and UCP2 have a structural homology of app. 60%. They execute their mitochondria uncoupling function through different molecular mechanisms. Non-shivering thermogenesis by UCP1 is mediated through a transmembrane dissipation of the proton motive force to create heat during sympathetic stimulation. UCP2, on the other hand, modulates through the interaction with methylated MICU1 the permeability of the cristae junction, which acts as an isolator for the cristae-located mitochondrial membrane potential. In this mini-review, we discuss and compare the recently described molecular mechanism of UCP1 in brown adipose tissue and UCP2 in aged and cancer non-excitable cells that contribute to mitochondrial uncoupling, and the synergistic effects of both UCPs with the mitochondrial Ca uptake machinery.

Address: Gottfried Schatz Research Center: Molecular Biology and Biochemistry, Medical University of Graz, Neue Stiftingtalstraße 6/4, Graz, 8010 Austria.; Gottfried Schatz Research Center: Molecular Biology and Biochemistry, Medical University of Graz, Neue Stiftingtalstraße 6/4, Graz, 8010 Austria; BioTechMed, Graz, Austria. Electronic address: [email protected].

DOI: 10.1016/j.ceca.2023.102736