ArticleThe EMBO journal2025
Proton conductance by human uncoupling protein 1 is inhibited by purine and pyrimidine nucleotides.
Article in The EMBO journal, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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The trial behind it
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Who cites it
8 citing papers in PubMed.
- UCP1-Dependent Thermogenic Adipose Tissue in Human Disease: Adipose-Centered Mechanisms, Biomarker Limitations, and Translational Perspectives.International journal of molecular sciences · 2026Review
- Article
- A Structural Context for the Mechanisms of Uncoupling Protein 1 in Brown Fat Thermogenesis.Acta physiologica (Oxford, England) · 2026Review
- Characterization of Recombinant GMPR fromBiology · 2026Article
- Current understanding and advances regarding the adipose-immune-metabolic axis in disease tolerance during sepsis.Frontiers in immunology · 2026Review
- Natural Mutation in Naked Mole-Rat UCP1 Refutes Importance of the Histidine Pair Motif for Proton Conductance and Thermogenesis.Acta physiologica (Oxford, England) · 2025Article
- Functional Complexity of Thermogenic Adipose Tissue: From Thermogenesis to Metabolic and Fibroinflammatory Crosstalk.International journal of molecular sciences · 2025Review
- The peculiar properties of mitochondrial carriers of the SLC25 family.The Biochemical journal · 2025Review
Corrections and comments
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Authors and funding
10 authors.
Funding
Abstract
Uncoupling protein 1 (UCP1, SLC25A7) is responsible for the thermogenic properties of brown adipose tissue. Upon fatty acid activation, UCP1 facilitates proton leakage, dissipating the mitochondrial proton motive force to release energy as heat. Purine nucleotides are considered to be the only inhibitors of UCP1 activity, binding to its central cavity to lock UCP1 in a proton-impermeable conformation. Here we show that pyrimidine nucleotides can also bind and inhibit its proton-conducting activity. All nucleotides bound in a pH-dependent manner, with the highest binding affinity observed for ATP, followed by dTTP, UTP, GTP and CTP. We also determined the structural basis of UTP binding to UCP1, showing that binding of purine and pyrimidine nucleotides follows the same molecular principles. We find that the closely related mitochondrial dicarboxylate carrier (SLC25A10) and oxoglutarate carrier (SLC25A11) have many cavity residues in common, but do not bind nucleotides. Thus, while UCP1 has evolved from dicarboxylate carriers, no selection for nucleobase specificity has occurred, highlighting the importance of the pH-dependent nucleotide binding mechanism mediated via the phosphate moieties.
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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.