The structure and function of the brown fat uncoupling protein UCP1: current status

Article type: Research Article

Authors: Rial, Eduardo^; | González‐Barroso, M. Mar | Fleury, Christophe | Bouillaud, Frédéric

Affiliations: Centro de Investigaciones Biológicas, C.S.I.C., Madrid, Spain | CEREMOD, C.N.R.S., Meudon, France

Note: [] Correspondence to: Dr Eduardo Rial, Centro de Investigaciones Biológicas, C.S.I.C., Velázquez 144, 28006 Madrid, Spain. Tel.: +3491 5611800, ext 4236; Fax: +3491 5627518; E‐mail: [email protected].

Abstract: The uncoupling protein of brown adipose tissue (UCP1) is a transporter that allows the dissipation as heat of the proton gradient generated by the respiratory chain. The discovery of new UCPs in other mammalian tissues and even in plants suggests that the proton permeability of the mitochondrial inner membrane can be regulated and its control is exerted by specialised proteins. The UCP1 is regulated both at the gene and the mitochondrial level to ensure a high thermogenic capacity to the tissue. The members of the mitochondrial transporter family, which includes the UCPs, present two behaviours with carrier and channel transport modes. It has been proposed that this property reflects a functional organization in two domains: a channel and a gating domain. Mounting evidence suggest that the matrix loops contribute to the formation of the gating domain and thus they are determinants to the control of transport activity.

Journal: Biofactors, vol. 8, no. 3-4, pp. 209-219, 1998