ArticleMolecular endocrinology (Baltimore, Md.)2016
Few Amino Acid Exchanges Expand the Substrate Spectrum of Monocarboxylate Transporter 10.
Article in Molecular endocrinology (Baltimore, Md.), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers, 1 of them a synthesis that pooled it.
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Who cites it
15 citing papers in PubMed, 1 synthesis or guideline pooled it, 23 citations in OpenAlex.
- Genome-wide analyses identify a role for SLC17A4 and AADAT in thyroid hormone regulation.Nature communications · 2018Pooled it
- Article
- Pathogenic MCT8V235L creates a steric clash that is alleviated by a compensating mutation of MCT8F285A.European thyroid journal · 2025Article
- Molecular mechanism of thyroxine transport by monocarboxylate transporters.Nature communications · 2025Article
- Structural insights into thyroid hormone transporter MCT8.Nature communications · 2025Article
- Mapping variants in thyroid hormone transporter MCT8 to disease severity by genomic, phenotypic, functional, structural and deep learning integration.Nature communications · 2025Article
- The influence of extended fasting on thyroid hormone: local and differentiated regulatory mechanisms.Frontiers in endocrinology · 2024Review
- Intrathyroidal feedforward and feedback network regulating thyroid hormone synthesis and secretion.Frontiers in endocrinology · 2022Review
- Monocarboxylate Transporters: Role and Regulation in Corneal Diabetes.Analytical cellular pathology (Amsterdam) · 2022Article
- A guide to plasma membrane solute carrier proteins.The FEBS journal · 2021Review
- Monocarboxylate Transporters (SLC16): Function, Regulation, and Role in Health and Disease.Pharmacological reviews · 2020Review
- Homology modeling and site-directed mutagenesis identify amino acid residues underlying the substrate selection mechanism of human monocarboxylate transporters 1 (hMCT1) and 4 (hMCT4).Cellular and molecular life sciences : CMLS · 2019Article
- Deafness and loss of cochlear hair cells in the absence of thyroid hormone transporters Slc16a2 (Mct8) and Slc16a10 (Mct10).Scientific reports · 2018Article
- Membrane-traversing mechanism of thyroid hormone transport by monocarboxylate transporter 8.Cellular and molecular life sciences : CMLS · 2017Article
- Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Monocarboxylate transporters (MCTs) belong to the SLC16 family within the major facilitator superfamily of transmembrane transporters. MCT8 is a thyroid hormone transporter mutated in the Allan-Herndon-Dudley syndrome, a severe psychomotor retardation syndrome. MCT10 is closely related to MCT8 and is known as T-type amino acid transporter. Both transporters mediate T3 transport, but although MCT8 also transports rT3 and T4, these compounds are not efficiently transported by MCT10, which, in contrast, transports aromatic amino acids. Based on the 58% amino acid identity within the transmembrane regions among MCT8 and MCT10, we reasoned that substrate specificity may be primarily determined by a small number of amino acid differences between MCT8 and MCT10 along the substrate translocation channel. Inspecting the homology model of MCT8 and a structure-guided alignment between both proteins, we selected 8 amino acid positions and prepared chimeric MCT10 proteins with selected amino acids changed to the corresponding amino acids in MCT8. The MCT10 mutant harboring 8 amino acid substitutions was stably expressed in Madin-Darby canine kidney 1 cells and found to exhibit T4 transport activity. We then successively reduced the number of amino acid substitutions and eventually identified a minimal set of 2-3 amino acid exchanges which were sufficient to allow T4 transport. The resulting MCT10 chimeras exhibited KM values for T4 similar to MCT8 but transported T4 at a slower rate. The acquisition of T4 transport by MCT10 was associated with complete loss of the capacity to transport Phe, when Tyr184 was mutated to Phe.
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