ArticleThe Journal of biological chemistry2012
Twelve transmembrane helices form the functional core of mammalian MATE1 (multidrug and toxin extruder 1) protein.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 44 citations in OpenAlex.
- Short-Chain and Long-Chain Fatty Acid-Containing Platinum-Acridine Anticancer Prodrugs: Exploiting Alternative Mechanisms of Cellular Internalization.Journal of medicinal chemistry · 2026Article
- Structural basis of drug recognition by human MATE1 transporter.Nature communications · 2025Article
- Platinum-Acridine Agents with High Activity in Cancers Expressing the Solute Carrier MATE1 (ACS medicinal chemistry letters · 2023Article
- The Alternating Access Mechanism in Mammalian Multidrug Resistance Transporters and Their Bacterial Homologs.Membranes · 2023Article
- Transport Turnover Rates for Human OCT2 and MATE1 Expressed in Chinese Hamster Ovary Cells.International journal of molecular sciences · 2022Article
- Why Should Metformin Not Be Given in Advanced Kidney Disease? Potential Leads from Computer Simulations.ACS omega · 2021Article
- A membrane transporter determines the spectrum of activity of a potent platinum-acridine hybrid anticancer agent.Scientific reports · 2020Article
- Glyphosate's Synergistic Toxicity in Combination with Other Factors as a Cause of Chronic Kidney Disease of Unknown Origin.International journal of environmental research and public health · 2019Review
- Current Advances in Studying Clinically Relevant Transporters of the Solute Carrier (SLC) Family by Connecting Computational Modeling and Data Science.Computational and structural biotechnology journal · 2019Review
- Arabidopsis MATE45 antagonizes local abscisic acid signaling to mediate development and abiotic stress responses.Plant direct · 2018Article
- The biosynthetic gene cluster for the cyanogenic glucoside dhurrin in Sorghum bicolor contains its co-expressed vacuolar MATE transporter.Scientific reports · 2016Article
- Lack of Influence of Substrate on Ligand Interaction with the Human Multidrug and Toxin Extruder, MATE1.Molecular pharmacology · 2016Article
- The first characterization of multidrug and toxin extrusion (MATE/SLC47) proteins in zebrafish (Danio rerio).Scientific reports · 2016Article
- Mechanisms for Two-Step Proton Transfer Reactions in the Outward-Facing Form of MATE Transporter.Biophysical journal · 2016Article
- The multidrug transporter MATE1 sequesters OCs within an intracellular compartment that has no influence on OC secretion in renal proximal tubules.American journal of physiology. Renal physiology · 2016Article
- Unstirred Water Layers and the Kinetics of Organic Cation Transport.Pharmaceutical research · 2015Article
- What do drug transporters really do?Nature reviews. Drug discovery · 2015Review
- Identification and expression analysis of MATE genes involved in flavonoid transport in blueberry plants.PloS one · 2015Article
- Substrate-dependent ligand inhibition of the human organic cation transporter OCT2.The Journal of pharmacology and experimental therapeutics · 2013Article
- Discovery of potent, selective multidrug and toxin extrusion transporter 1 (MATE1, SLC47A1) inhibitors through prescription drug profiling and computational modeling.Journal of medicinal chemistry · 2013Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
The x-ray structure of the prototypic MATE family member, NorM from Vibrio cholerae, reveals a protein fold composed of 12 transmembrane helices (TMHs), confirming hydropathy analyses of the majority of (prokaryotic and plant) MATE transporters. However, the mammalian MATEs are generally predicted to have a 13(th) TMH and an extracellular C terminus. Here we affirm this prediction, showing that the C termini of epitope-tagged, full-length human, rabbit, and mouse MATE1 were accessible to antibodies from the extracellular face of the membrane. Truncation of these proteins at or near the predicted junction between the 13(th) TMH and the long cytoplasmic loop that precedes it resulted in proteins that (i) trafficked to the membrane and (ii) interacted with antibodies only after permeabilization of the plasma membrane. CHO cells expressing rbMate1 truncated at residue Gly-545 supported levels of pH-sensitive transport similar to that of cells expressing the full-length protein. Although the high transport rate of the Gly-545 truncation mutant was associated with higher levels of membrane expression (than full-length MATE1), suggesting the 13(th) TMH may influence substrate translocation, the selectivity profile of the mutant indicated that TMH13 has little impact on ligand binding. We conclude that the functional core of MATE1 consists of 12 (not 13) TMHs. Therefore, we used the x-ray structure of NorM to develop a homology model of the first 12 TMHs of MATE1. The model proved to be stable in molecular dynamic simulations and agreed with topology evident from preliminary cysteine scanning of intracellular versus extracellular loops.
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