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Fatty Acid Interaction with Mitochondrial Uncoupling Proteins

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Abstract

The phenomena of fatty acid interaction with mitochondrial integral membrane proteins, namelyuncoupling proteins (UCPs), are reviewed to emphasize the fatty acid cycling mechanism thathas been suggested to explain the UCP function. Fatty acid-induced uncoupling is suggestedto serve in bioenergetic systems, to set the optimum efficiency, and to tune the degree ofcoupling of oxidative phosphorylation. Fatty acid interaction with the “classic” uncouplingprotein (UCP1) from mitochondria of thermogenic brown adipose tissue (BAT) is well known.UCP1 is considered to mediate purine nucleotide-sensitive uniport of monovalent unipolaranions, including anionic fatty acids. The return of protonated fatty acid leads to H+ uniportand uncoupling. Experiments supporting this mechanism are also reviewed for plant uncouplingmitochondrial protein (PUMP) and ADP/ATP carrier. The fatty acid cycling mechanism ispredicted, as well for the recently discovered uncoupling proteins, UCP2 and UCP3.

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  1. Institute of Physiology, Department of Membrane Transport Biophysics, Academy of Sciences of the Czech Republic, Vídenňská 1083, CZ 14220, Prague, Czech Republic

    Petr Ježek

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Ježek, P. Fatty Acid Interaction with Mitochondrial Uncoupling Proteins. J Bioenerg Biomembr 31, 457–466 (1999). https://doi.org/10.1023/A:1005496306893

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