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Oflaz, FE; Koshenov, Z; Hirtl, M; Bachkoenig, OA; Graier, WF; Gottschalk, B.
Synergy of uncoupling proteins (1 and 2) with mitochondrial Ca2+ uptake machinery potentiate mitochondrial uncoupling.
Cell Calcium. 2023; 112:102736 Doi: 10.1016/j.ceca.2023.102736
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Leading authors Med Uni Graz
Graier Wolfgang
Oflaz Furkan Enes
Co-authors Med Uni Graz
Bachkönig Olaf Arne Georg
Gottschalk Benjamin
Hirtl Martin
Koshenov Zhanat
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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 Ca2+ uptake machinery.
Find related publications in this database (using NLM MeSH Indexing)
Mitochondrial Uncoupling Proteins - metabolism
Membrane Proteins - metabolism
Ion Channels - metabolism
Mitochondrial Proteins - metabolism
Uncoupling Protein 2 - metabolism
Mitochondria - metabolism

Find related publications in this database (Keywords)
Uncoupling protein 1
Uncoupling protein 2
MitochondrialCa2+uptake machinery
Mitochondrial uncoupling
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