Thermogenin is a mitochondrial carrier protein found in brown adipose tissue (BAT). It is used to generate heat by non-shivering thermogenesis, and makes a quantitatively important contribution to countering heat loss in babies which would otherwise occur due to their high surface area-volume ratio.
An uncoupling protein (UCP) is a mitochondrial inner membrane protein that is a regulated proton channel or transporter. An uncoupling protein is thus capable of dissipating the proton gradient generated by NADH-powered pumping of protons from the mitochondrial matrix to the mitochondrial intermembrane space. The energy lost in dissipating the proton gradient via UCPs is not used to do biochemical work. Instead, heat is generated. This is what links UCP to thermogenesis. However, not every type of UCPs are related to thermogenesis. Although UCP2 and UCP3 are closely related to UCP1, UCP2 and UCP3 do not affect thermoregulatory abilities of vertebrates. UCPs are positioned in the same membrane as the ATP synthase, which is also a proton channel. The two proteins thus work in parallel with one generating heat and the other generating ATP from ADP and inorganic phosphate, the last step in oxidative phosphorylation. Mitochondria respiration is coupled to ATP synthesis, but is regulated by UCPs. UCPs belong to the mitochondrial carrier (SLC25) family.
Mitochondrial uncoupling protein 3 is a protein that in humans is encoded by the UCP3 gene. The gene is located in chromosome (11q13.4) with an exon count of 7 and is expressed on the inner mitochondrial membrane. Uncoupling proteins transfer anions from the inner mitochondrial membrane to the outer mitochondrial membrane, thereby separating oxidative phosphorylation from synthesis of ATP, and dissipating energy stored in the mitochondrial membrane potential as heat. Uncoupling proteins also reduce generation of reactive oxygen species.
Leptin receptor, also known as LEP-R or OB-R, is a type I cytokine receptor, a protein that in humans is encoded by the LEPR gene. LEP-R functions as a receptor for the fat cell-specific hormone leptin. LEP-R has also been designated as CD295. Its location is the cell membrane, and it has extracellular, trans-membrane and intracellular sections.
G-protein coupled receptor 3 is a protein that in humans is encoded by the GPR3 gene. The protein encoded by this gene is a member of the G protein-coupled receptor family of transmembrane receptors and is involved in signal transduction.
Anion exchange protein 2 (AE2) is a membrane transport protein that in humans is encoded by the SLC4A2 gene. AE2 is functionally similar to the Band 3 Cl−/HCO3− exchange protein.
Selenoprotein S, also known as SELS, is a human gene.
Solute carrier family 22 member 11 is a protein that in humans is encoded by the SLC22A11 gene.
Sodium-coupled neutral amino acid transporter 2 is a protein that in humans is encoded by the SLC38A2 gene.
Mitochondrial import receptor subunit TOM34 is a protein that in humans is encoded by the TOMM34 gene.
Mitofusin-1 is a protein that in humans is encoded by the MFN1 gene.
Autophagy related 12 is a protein that in humans is encoded by the ATG12 gene.
Aquaporin-7 (AQP-7) is a protein that in humans is encoded by the AQP7 gene.
The ATP5MC2 gene is one of three human paralogs that encode membrane subunit c of the mitochondrial ATP synthase.
Brain mitochondrial carrier protein 1 is a protein that in humans is encoded by the SLC25A14 gene.
Mitochondrial uncoupling protein 4 is a protein that in humans is encoded by the SLC25A27 gene.
The ATP5MC3 gene is one of three human paralogs that encode membrane subunit c of the mitochondrial ATP synthase.
ADP/ATP translocase 2 is a protein that in humans is encoded by the SLC25A5 gene on the X chromosome.
Peptidase M20 domain containing 1 is a circulating enzyme which in humans is encoded by the PM20D1 gene. PM20D1 regulates bioactive N-acyl amide lipids and has been implicated in obesity, type 2 diabetes, pain, and Alzheimer's disease.
Daniel Ricquier, is a French biochemist known for his work in mitochondria and hereditary metabolic diseases. Ricquier has been a member of the French Academy of Sciences since 2002, and a professor of biochemistry and Molecular Biology at the Faculty of Medicine of the University of Paris Descartes since 2003.
