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Bouillaud, Frédéric; Alves-Guerra, Marie-Clotilde; Ricquier, Daniel
Biochimica et biophysica acta, October 2016, 2016-10-00, 2016-10, Letnik: 1863, Številka: 10Journal Article
The first member of the uncoupling protein (UCP) family, brown adipose tissue uncoupling protein 1 (UCP1), was identified in 1976. Twenty years later, two closely related proteins, UCP2 and UCP3, were described in mammals. Homologs of these proteins exist in other organisms, including plants. Uncoupling refers to a deterioration of energy conservation between substrate oxidation and ADP phosphorylation. Complete energy conservation loss would be fatal but fine-tuning can be beneficial for processes such as thermogenesis, redox control, and prevention of mitochondrial ROS release. The coupled/uncoupled state of mitochondria is related to the permeability of the inner membrane and the proton transport mediated by activated UCPs underlies the uncoupling activity of these proteins. Proton transport by UCP1 is activated by fatty acids and this ensures thermogenesis. In vivo in absence of this activation UCP1 remains inhibited with no transport activity. A similar situation now seems unlikely for UCP2 and UCP3 and while activation of their proton transport has been described its physiological relevance remains uncertain and their influence can be envisaged as a result of another transport pathway that takes place in the absence of activation. This article is part of a Special Issue entitled: Mitochondrial Channels edited by Pierre Sonveaux, Pierre Maechler and Jean-Claude Martinou. •UCP denotes ‘UnCoupling Protein’ a term coined for UCP1 in brown adipose tissue.•Uncoupling degrades energy conservation (ATP yield) in mitochondria.•Uncoupling could also target thermogenesis (UCP1) or redox control (other UCPs).•Uncoupling relies on proton transport by the UCPs and requires activation.•UCP2/3 in absence of activation are likely to perform other transport activities.
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