ArticlePloS one2021
Basigin drives intracellular accumulation of l-lactate by harvesting protons and substrate anions.
Article in PloS one, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 25 citations in OpenAlex.
- Phenylalanine Versus Tyrosine (Pos. 367/332 in MCT1/MCT4) in the Substrate Binding Site Defines Affinity and Preferred Directionality of Human Monocarboxylate Transporters 1-4.Acta physiologica (Oxford, England) · 2026Article
- Intrinsic Asymmetry in Weak Acid Transmembrane Transporters.Biomolecules · 2026Review
- Basigin links altered skeletal stem cell lineage dynamics with glucocorticoid-induced bone loss and impaired angiogenesis.Nature communications · 2025Article
- Article
- A basigin antibody modulates MCTs to impact tumor metabolism and immunity.Cell discovery · 2025Article
- A Yeast-Based Assay for Inhibitors of l-Lactate Transport Utilizing Fluorescent Biosensors.ChemMedChem · 2025Article
- Lactate-mediated metabolic reprogramming of tumor-associated macrophages: implications for tumor progression and therapeutic potential.Frontiers in immunology · 2025Review
- SARS-CoV-2 Is an Electricity-Driven Virus.Reviews of physiology, biochemistry and pharmacology · 2025Review
- Red blood cell signaling is functionally conserved iniScience · 2024Article
- Severely polarized extracellular acidity around tumour cells.Nature biomedical engineering · 2024Article
- Basigin mediation of Plasmodium falciparum red blood cell invasion does not require its transmembrane domain or interaction with monocarboxylate transporter 1.PLoS pathogens · 2024Article
- CD147/Basigin Is Involved in the Development of Malignant Tumors and T-Cell-Mediated Immunological Disorders via Regulation of Glycolysis.International journal of molecular sciences · 2023Review
- Human monocarboxylate transporters accept and relay protons via the bound substrate for selectivity and activity at physiological pH.PNAS nexus · 2023Article
- Local Attraction of Substrates and Co-Substrates Enhances Weak Acid and Base Transmembrane Transport.Biomolecules · 2022Review
- Lactic Acid Permeability of Aquaporin-9 Enables Cytoplasmic Lactate Accumulation via an Ion Trap.Life (Basel, Switzerland) · 2022Article
- Metabolic Transporters in the Peripheral Nerve-What, Where, and Why?Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2021Review
- Strategies to identify, engineer, and validate antibodies targeting blood-brain barrier receptor-mediated transcytosis systems for CNS drug delivery.Expert opinion on drug deliveryReview
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Transmembrane transport of l-lactate by members of the monocarboxylate transporter family, MCT, is vital in human physiology and a malignancy factor in cancer. Interaction with an accessory protein, typically basigin, is required to deliver the MCT to the plasma membrane. It is unknown whether basigin additionally exerts direct effects on the transmembrane l-lactate transport of MCT1. Here, we show that the presence of basigin leads to an intracellular accumulation of l-lactate 4.5-fold above the substrate/proton concentrations provided by the external buffer. Using basigin truncations we localized the effect to arise from the extracellular Ig-I domain. Identification of surface patches of condensed opposite electrostatic potential, and experimental analysis of charge-affecting Ig-I mutants indicated a bivalent harvesting antenna functionality for both, protons and substrate anions. From these data, and determinations of the cytosolic pH with a fluorescent probe, we conclude that the basigin Ig-I domain drives lactate uptake by locally increasing the proton and substrate concentration at the extracellular MCT entry site. The biophysical properties are physiologically relevant as cell growth on lactate media was strongly promoted in the presence of the Ig-I domain. Lack of the domain due to shedding, or misfolding due to breakage of a stabilizing disulfide bridge reversed the effect. Tumor progression according to classical or reverse Warburg effects depends on the transmembrane l-lactate distribution, and this study shows that the basigin Ig-I domain is a pivotal determinant.
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