ReviewBiochimie2017
The molecular features of uncoupling protein 1 support a conventional mitochondrial carrier-like mechanism.
Review in Biochimie, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers, 1 of them a synthesis that pooled it.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
62 citing papers in PubMed, 1 synthesis or guideline pooled it, 140 citations in OpenAlex.
- Unraveling the rationale and conducting a comprehensive assessment of KD025 (Belumosudil) as a candidate drug for inhibiting adipogenic differentiation-a systematic review.Naunyn-Schmiedeberg's archives of pharmacology · 2024Pooled it
- Article
- A Structural Context for the Mechanisms of Uncoupling Protein 1 in Brown Fat Thermogenesis.Acta physiologica (Oxford, England) · 2026Review
- Ultrastructural characterization of white adipocytes in a mouse model with enhanced sequestration of fatty acids in adipose tissue.Adipocyte · 2025Article
- Interactions of Arachidonic Acid with AAC1 and UCP1.International journal of molecular sciences · 2025Article
- Natural Mutation in Naked Mole-Rat UCP1 Refutes Importance of the Histidine Pair Motif for Proton Conductance and Thermogenesis.Acta physiologica (Oxford, England) · 2025Article
- The peculiar properties of mitochondrial carriers of the SLC25 family.The Biochemical journal · 2025Review
- Article
- NOTCH Signaling Networks in Perivascular Adipose Tissue.Arteriosclerosis, thrombosis, and vascular biology · 2025Review
- Metabolic signals in sleep regulation: the role of brown adipose tissue.Neurobiology of sleep and circadian rhythms · 2025Article
- Proton conductance by human uncoupling protein 1 is inhibited by purine and pyrimidine nucleotides.The EMBO journal · 2025Article
- Brown Adipose Tissue Mimicking Head and Neck Cancer on PET Scan in a Patient on GLP-1 Drug.The Laryngoscope · 2025Article
- Hypoxia-inducible factor-1α-deficient adipose-tissue macrophages produce the heat to mediate lipolysis of white adipose tissue through uncoupling protein-1.Laboratory animal research · 2024Article
- Cryptotanshinone promotes brown fat activity by AMPK activation to inhibit obesity.Nutrition research and practice · 2024Article
- Mitochondrial dysfunction in the pathogenesis of endothelial dysfunction.Molecular and cellular biochemistry · 2024Review
- Terrestrial Birth and Body Size Tune UCP1 Functionality in Seals.Molecular biology and evolution · 2024Article
- Article
- Metal Uptake by Mitochondrial Carrier Family Proteins Using Lactococcus lactis.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Article
- Article
2 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 3 institutions in 1 country.
Funding
Abstract
Uncoupling protein 1 (UCP1) is an integral membrane protein found in the mitochondrial inner membrane of brown adipose tissue, and facilitates the process of non-shivering thermogenesis in mammals. Its activation by fatty acids, which overcomes its inhibition by purine nucleotides, leads to an increase in the proton conductance of the inner mitochondrial membrane, short-circuiting the mitochondrion to produce heat rather than ATP. Despite 40 years of intense research, the underlying molecular mechanism of UCP1 is still under debate. The protein belongs to the mitochondrial carrier family of transporters, which have recently been shown to utilise a domain-based alternating-access mechanism, cycling between a cytoplasmic and matrix state to transport metabolites across the inner membrane. Here, we review the protein properties of UCP1 and compare them to those of mitochondrial carriers. UCP1 has the same structural fold as other mitochondrial carriers and, in contrast to past claims, is a monomer, binding one purine nucleotide and three cardiolipin molecules tightly. The protein has a single substrate binding site, which is similar to those of the dicarboxylate and oxoglutarate carriers, but also contains a proton binding site and several hydrophobic residues. As found in other mitochondrial carriers, UCP1 has two conserved salt bridge networks on either side of the central cavity, which regulate access to the substrate binding site in an alternating way. The conserved domain structures and mobile inter-domain interfaces are consistent with an alternating access mechanism too. In conclusion, UCP1 has retained all of the key features of mitochondrial carriers, indicating that it operates by a conventional carrier-like mechanism.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.