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Journal articles on the topic 'MATE transporter'

Author: Grafiati

Published: 4 June 2021

Last updated: 7 February 2022

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1

Goda, Mitsuhiro, Kana Oda, Atsuko Oda, Naoki Kobayashi, and Masato Otsuka. "Involvement of the Multidrug and Toxic Compound Extrusion Transporter in Testosterone Release from Cultured Pig Leydig Cells." Pharmacology 100, no. 1-2 (2017): 31–39. http://dx.doi.org/10.1159/000460822.

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Testosterone is considered to be released from Leydig cells via passive diffusion because of its hydrophobicity; however, the exact mechanism underlying testosterone secretion and the transporter involved are both unknown. Multidrug and toxic compound extrusion (MATE) transporters are predominantly found in the kidneys and liver and are thought to function in the elimination of metabolic organic cations during the final step of excretion in the kidney. In contrast, mMATE2 has been shown to be predominantly expressed in testicular Leydig cells. Although the physiological function of mMATE2 in Leydig cells is unknown, we hypothesized that mMATE2 acts as a testosterone exporter and is responsible for the secretion of testosterone from Leydig cells. Therefore, in the present study, we investigated the involvement of the MATE transporter in testosterone secretion from pig Leydig cells. Immunohistochemical analysis with anti-pig MATE2 antiserum indicated that the MATE transporter is present in pig Leydig cells. Additionally, treatment with the MATE inhibitors cimetidine and pyrimethamine reduced the testosterone secretion from pig Leydig cells but increased the intracellular testosterone levels. Estradiol release and intracellular estradiol level induced by human chorionic gonadotropin (hCG) further increased with cimetidine treatment. These results indicated that testosterone produced by hCG treatment is secreted from Leydig cells via the MATE transporter; however, in the presence of cimetidine or pyrimethamine, this MATE transporter-mediated secretion was inhibited, resulting in increased intracellular testosterone levels and estradiol production in Leydig cells. Thus, the MATE transporter may be responsible for testosterone secretion from Leydig cells.

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2

Tocci, Nadia, Francesco Iannelli, Alessandro Bidossi, Maria Laura Ciusa, Francesca Decorosi, Carlo Viti, Gianni Pozzi, Susanna Ricci, and Marco Rinaldo Oggioni. "Functional Analysis of Pneumococcal Drug Efflux Pumps Associates the MATE DinF Transporter with Quinolone Susceptibility." Antimicrobial Agents and Chemotherapy 57, no. 1 (October 31, 2012): 248–53. http://dx.doi.org/10.1128/aac.01298-12.

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ABSTRACTThe pneumococcal chromosome encodes about 140 transporters, many of which are predicted to be involved in efflux. In order to critically evaluate pneumococcal efflux, a series of transporter mutants were constructed, and their phenotypes were assayed by disk diffusion, microdilution drug susceptibility testing (MIC testing), growth of cultures at sub-MIC concentrations, and phenotype microarray analysis. Mutants with mutations in seven ATP binding cassette (ABC) transporters, three multiantimicrobial extrusion (MATE) family efflux pumps, and one major facilitator superfamily (MFS) transporter were obtained inStreptococcus pneumoniaestrain DP1004. The susceptibility of these 11 mutants to over 250 different substances was compared to that of the parent strain. Of the tested transporters, only the ABC transporter PatAB (SP2073-5) presented a clear multidrug resistance (MDR) profile, as the mutant showed significantly increased susceptibility to ethidium bromide, acriflavine, and berberine. Among the other transporters analyzed, the mutants devoid of the MATE efflux pump SP2065 exhibited reduced susceptibility to novobiocin, and those with mutations of the MATE family DinF transport system (SP1939) exhibited increased susceptibility to moxifloxacin, ciprofloxacin, and levofloxacin. This change in quinolone MIC was found to be independent from the competence-mediated effect of quinolones on thecinA-recA-dinFoperon. Furthermore, thedinFmutant, in contrast to the parental strain, allowed selection for quinolone-resistant mutants when exposed to moxifloxacin. These data confirm the clear MDR profile of the PatAB ABC transporter and suggest for the MATE DinF a phenotype associated with quinolone susceptibility, particularly for moxifloxacin.

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3

Zakrzewska, Sandra, Ahmad Reza Mehdipour, Viveka Nand Malviya, Tsuyoshi Nonaka, Juergen Koepke, Cornelia Muenke, Winfried Hausner, Gerhard Hummer, Schara Safarian, and Hartmut Michel. "Inward-facing conformation of a multidrug resistance MATE family transporter." Proceedings of the National Academy of Sciences 116, no. 25 (June 3, 2019): 12275–84. http://dx.doi.org/10.1073/pnas.1904210116.

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Multidrug and toxic compound extrusion (MATE) transporters mediate excretion of xenobiotics and toxic metabolites, thereby conferring multidrug resistance in bacterial pathogens and cancer cells. Structural information on the alternate conformational states and knowledge of the detailed mechanism of MATE transport are of great importance for drug development. However, the structures of MATE transporters are only known in V-shaped outward-facing conformations. Here, we present the crystal structure of a MATE transporter from Pyrococcus furiosus (PfMATE) in the long-sought-after inward-facing state, which was obtained after crystallization in the presence of native lipids. Transition from the outward-facing state to the inward-facing state involves rigid body movements of transmembrane helices (TMs) 2–6 and 8–12 to form an inverted V, facilitated by a loose binding of TM1 and TM7 to their respective bundles and their conformational flexibility. The inward-facing structure of PfMATE in combination with the outward-facing one supports an alternating access mechanism for the MATE family transporters.

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4

Väisänen, Enni, Junko Takahashi, Ogonna Obudulu, Joakim Bygdell, Pirkko Karhunen, Olga Blokhina, Teresa Laitinen, et al. "Hunting monolignol transporters: membrane proteomics and biochemical transport assays with membrane vesicles of Norway spruce." Journal of Experimental Botany 71, no. 20 (August 10, 2020): 6379–95. http://dx.doi.org/10.1093/jxb/eraa368.

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Abstract Both the mechanisms of monolignol transport and the transported form of monolignols in developing xylem of trees are unknown. We tested the hypothesis of an active, plasma membrane-localized transport of monolignol monomers, dimers, and/or glucosidic forms with membrane vesicles prepared from developing xylem and lignin-forming tissue-cultured cells of Norway spruce (Picea abies L. Karst.), as well as from control materials, comprising non-lignifying Norway spruce phloem and tobacco (Nicotiana tabacum L.) BY-2 cells. Xylem and BY-2 vesicles transported both coniferin and p-coumaryl alcohol glucoside, but inhibitor assays suggested that this transport was through the tonoplast. Membrane vesicles prepared from lignin-forming spruce cells showed coniferin transport, but the Km value for coniferin was much higher than those of xylem and BY-2 cells. Liquid chromatography-mass spectrometry analysis of membrane proteins isolated from spruce developing xylem, phloem, and lignin-forming cultured cells revealed multiple transporters. These were compared with a transporter gene set obtained by a correlation analysis with a selected set of spruce monolignol biosynthesis genes. Biochemical membrane vesicle assays showed no support for ABC-transporter-mediated monolignol transport but point to a role for secondary active transporters (such as MFS or MATE transporters). In contrast, proteomic and co-expression analyses suggested a role for ABC transporters and MFS transporters.

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5

Kusakizako, Tsukasa, Yoshiki Tanaka, Christopher J. Hipolito, Teruo Kuroda, Ryuichiro Ishitani, Hiroaki Suga, and Osamu Nureki. "LCP crystallization and X-ray diffraction analysis of VcmN, a MATE transporter fromVibrio cholerae." Acta Crystallographica Section F Structural Biology Communications 72, no. 7 (June 22, 2016): 552–57. http://dx.doi.org/10.1107/s2053230x16008931.

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Multidrug and toxic compound extrusion (MATE) transporters, one of the multidrug exporter families, efflux xenobiotics towards the extracellular side of the membrane. Since MATE transporters expressed in bacterial pathogens contribute to multidrug resistance, they are important therapeutic targets. Here, a MATE-transporter homologue fromVibrio cholerae, VcmN, was overexpressed inEscherichia coli, purified and crystallized in lipidic cubic phase (LCP). X-ray diffraction data were collected to 2.5 Å resolution from a single crystal obtained in a sandwich plate. The crystal belonged to space groupP212121, with unit-cell parametersa= 52.3,b= 93.7,c= 100.2 Å. As a result of further LCP crystallization trials, crystals of larger size were obtained using sitting-drop plates. X-ray diffraction data were collected to 2.2 Å resolution from a single crystal obtained in a sitting-drop plate. The crystal belonged to space groupP212121, with unit-cell parametersa= 61.9,b= 91.8,c= 100.9 Å. The present work provides valuable insights into the atomic resolution structure determination of membrane transporters.

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6

Chen, Jing, Yuji Morita, M. Nazmul Huda, Teruo Kuroda, Tohru Mizushima, and Tomofusa Tsuchiya. "VmrA, a Member of a Novel Class of Na+-Coupled Multidrug Efflux Pumps from Vibrio parahaemolyticus." Journal of Bacteriology 184, no. 2 (January 15, 2002): 572–76. http://dx.doi.org/10.1128/jb.184.2.572-576.2002.

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ABSTRACT Gene vmrA, cloned from Vibrio parahaemolyticus, made Escherichia coli resistant to 4prime;,6-diamino-2-phenylindol, tetraphenylphosphonium chloride, acriflavine, and ethidium bromide. VmrA belongs to the DinF branch of MATE family efflux transporters. VmrA catalyzed acriflavine efflux and showed Na+/drug transporter activity because the addition of tetraphenylphosphonium to Na+-loaded cells caused Na+ efflux.

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7

Freitas-Lima, Leandro Ceotto, Alexandre Budu, Adriano Cleis Arruda, Mauro Sérgio Perilhão, Jonatan Barrera-Chimal, Ronaldo Carvalho Araujo, and Gabriel Rufino Estrela. "PPAR-α Deletion Attenuates Cisplatin Nephrotoxicity by Modulating Renal Organic Transporters MATE-1 and OCT-2." International Journal of Molecular Sciences 21, no. 19 (October 8, 2020): 7416. http://dx.doi.org/10.3390/ijms21197416.

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Cisplatin is a chemotherapy drug widely used in the treatment of solid tumors. However, nephrotoxicity has been reported in about one-third of patients undergoing cisplatin therapy. Proximal tubules are the main target of cisplatin toxicity and cellular uptake; elimination of this drug can modulate renal damage. Organic transporters play an important role in the transport of cisplatin into the kidney and organic cations transporter 2 (OCT-2) has been shown to be one of the most important transporters to play this role. On the other hand, multidrug and toxin extrusion 1 (MATE-1) transporter is the main protein that mediates the extrusion of cisplatin into the urine. Cisplatin nephrotoxicity has been shown to be enhanced by increased OCT-2 and/or reduced MATE-1 activity. Peroxisome proliferator-activated receptor alpha (PPAR-α) is the transcription factor which controls lipid metabolism and glucose homeostasis; it is highly expressed in the kidneys and interacts with both MATE-1 and OCT-2. Considering the above, we treated wild-type and PPAR-α knockout mice with cisplatin in order to evaluate the severity of nephrotoxicity. Cisplatin induced renal dysfunction, renal inflammation, apoptosis and tubular injury in wild-type mice, whereas PPAR-α deletion protected against these alterations. Moreover, we observed that cisplatin induced down-regulation of organic transporters MATE-1 and OCT-2 and that PPAR-α deletion restored the expression of these transporters. In addition, PPAR-α knockout mice at basal state showed increased MATE-1 expression and reduced OCT-2 levels. Here, we show for the first time that PPAR-α deletion protects against cisplatin nephrotoxicity and that this protection is via modulation of the organic transporters MATE-1 and OCT-2.

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8

Kusakizako, Tsukasa, Yoshiki Tanaka, Andrés Maturana, Christopher Hipolito, Teruo Kuroda, Ryuichiro Ishitani, Hiroaki Suga, and Osamu Nureki. "X-ray crystallographic analysis of a MATE multidrug transporter from V. cholerae." Acta Crystallographica Section A Foundations and Advances 70, a1 (August 5, 2014): C709. http://dx.doi.org/10.1107/s2053273314092900.

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MATE (Multidrug And Toxic compound Extrusion) family transporters are highly conserved from Bacteria to Eukarya including human, and export a broad range of xenobiotics using either a proton or a sodium ion gradient across the membrane. Especially in bacterial pathogens, MATE transporters contribute to their multiple drug resistance (MDR). To understand how MATE transporters export various substrates such as drugs and thus how pathogens acquire MDR, structural analyses are essential. The crystal structures of several MATE transporters from pathogens have been reported. However, because of the limited resolution and the lack of drug-MATE transporters complex structures, the recognition mechanism of various substrates and the coupling mechanism of the cation influx and the drug efflux have been poorly understood. Although the high-resolution structures of MATE transporters from non-pathogenic archaeal P. furiosus (PfMATE) have been reported, PfMATE shares low sequence identity with MATE transporters from pathogens such as V. cholerae. Therefore, further findings of the structural mechanism of MDR caused by MATE transporters from pathogens have been needed. To understand the substrate recognition and transport mechanism of MATE transporters from pathogens, we determined the crystal structures of one of MATE transporters from V. cholerae (VcMATE) at 2.5-2.7 Å resolutions using in meso crystallization method. The high-resolution structures of VcMATE show two distinct conformations, as observed in the structures of PfMATE, and reveal the large movement of transmembrane helix 1 and the putative substrate-binding site. The structures suggest that the bending of transmembrane helix 1 and the sequential collapse of the putative substrate-binding site induce the release of the bound substrate. This conformational change during the substrate transport may be a common mechanism among MATE transporters from pathogens to non-pathogens.

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9

Dobritzsch, Melanie, Tilo Lübken, Lennart Eschen-Lippold, Karin Gorzolka, Elke Blum, Andreas Matern, Sylvestre Marillonnet, Christoph Böttcher, Birgit Dräger, and Sabine Rosahl. "MATE Transporter-Dependent Export of Hydroxycinnamic Acid Amides." Plant Cell 28, no. 2 (January 7, 2016): 583–96. http://dx.doi.org/10.1105/tpc.15.00706.

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10

Meyer zu Schwabedissen, Henriette E., Celine Verstuyft, Heyo K. Kroemer, Laurent Becquemont, and Richard B. Kim. "Human multidrug and toxin extrusion 1 (MATE1/SLC47A1) transporter: functional characterization, interaction with OCT2 (SLC22A2), and single nucleotide polymorphisms." American Journal of Physiology-Renal Physiology 298, no. 4 (April 2010): F997—F1005. http://dx.doi.org/10.1152/ajprenal.00431.2009.

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renal elimination of a number of cationic compounds is thought to be mediated by the organic cation transporter 2 (OCT2, SLC22A2), a drug uptake transporter expressed at the basolateral domain of renal tubular cells. Recently, the key efflux transporter for the secretion organic cations was identified as an electroneutral H+/organic cation exchanger termed the multidrug and toxin extrusion (MATE)-type transporter 1 (MATE1, SLC47A1). The key goals of this study were to assess the interplay between the renal cationic transporters OCT2 and MATE1 and the functional assessment of genetic variation in human MATE1. First, the ability of various agents to interact with OCT2- or MATE1-mediated transport was determined using a recombinant vaccinia expression system. We were able to identify several drugs in clinical use with a divergent inhibitory capacity for these transporters. Subsequently, we further assessed the effect of those compounds on the cellular accumulation of shared substrates using OCT2 and MATE1 double-transfected cells. Consistent with data obtained using single transporter transfected cells, compounds that exhibited preferential inhibition of MATE1 such as rapamycin and mitoxantrone induced significant cellular accumulation of cationic substrates. We next assessed the functional relevance of MATE1 genetic polymorphisms. Significant loss of transport activity for metformin and tetraethylammonium was noted for two nonsynonymous single nucleotide polymorphisms (SNPs), c.404T>C (p.159T>M) and c.1012G>A (p.338V>A). The c.404T>C was only seen in Asian subjects with an allele frequency of 1%, and the c.1012G>A SNP was much more common, especially among those of African descent. In conclusion, we show that coordinate function of MATE1 with OCT2 likely contributes to the vectorial renal elimination of organic cationic drugs and that altered activity of MATE1, whether by drugs or polymorphisms, should be considered as an important determinant of renal cationic drug elimination.

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11

Zhang, Haiwen, Fu-Geng Zhao, Ren-Jie Tang, Yuexuan Yu, Jiali Song, Yuan Wang, Legong Li, and Sheng Luan. "Two tonoplast MATE proteins function as turgor-regulating chloride channels inArabidopsis." Proceedings of the National Academy of Sciences 114, no. 10 (February 15, 2017): E2036—E2045. http://dx.doi.org/10.1073/pnas.1616203114.

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The central vacuole in a plant cell occupies the majority of the cellular volume and plays a key role in turgor regulation. The vacuolar membrane (tonoplast) contains a large number of transporters that mediate fluxes of solutes and water, thereby adjusting cell turgor in response to developmental and environmental signals. We report that two tonoplast Detoxification efflux carrier (DTX)/Multidrug and Toxic Compound Extrusion (MATE) transporters, DTX33 and DTX35, function as chloride channels essential for turgor regulation inArabidopsis. Ectopic expression of each transporter inNicotiana benthamianamesophyll cells elicited a large voltage-dependent inward chloride current across the tonoplast, showing that DTX33 and DTX35 each constitute a functional channel. Both channels are highly expressed inArabidopsistissues, including root hairs and guard cells that experience rapid turgor changes during root-hair elongation and stomatal movements. Disruption of these two genes, either in single or double mutants, resulted in shorter root hairs and smaller stomatal aperture, with double mutants showing more severe defects, suggesting that these two channels function additively to facilitate anion influx into the vacuole during cell expansion. In addition,dtx35single mutant showed lower fertility as a result of a defect in pollen-tube growth. Indeed, patch-clamp recording of isolated vacuoles indicated that the inward chloride channel activity across the tonoplast was impaired in the double mutant. Because MATE proteins are widely known transporters of organic compounds, finding MATE members as chloride channels expands the functional definition of this large family of transporters.

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12

Jagessar, Kevin L., Derek P. Claxton, Richard A. Stein, and Hassane S. Mchaourab. "Sequence and structural determinants of ligand-dependent alternating access of a MATE transporter." Proceedings of the National Academy of Sciences 117, no. 9 (February 19, 2020): 4732–40. http://dx.doi.org/10.1073/pnas.1917139117.

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Multidrug and toxic compound extrusion (MATE) transporters are ubiquitous ion-coupled antiporters that extrude structurally and chemically dissimilar cytotoxic compounds and have been implicated in conferring multidrug resistance. Here, we integrate double electron–electron resonance (DEER) with functional assays and site-directed mutagenesis of conserved residues to illuminate principles of ligand-dependent alternating access of PfMATE, a proton-coupled MATE from the hyperthermophilic archaeonPyrococcus furiosus. Pairs of spin labels monitoring the two sides of the transporter reconstituted into nanodiscs reveal large-amplitude movement of helices that alter the orientation of a putative substrate binding cavity. We found that acidic pH favors formation of an inward-facing (IF) conformation, whereas elevated pH (>7) and the substrate rhodamine 6G stabilizes an outward-facing (OF) conformation. The lipid-dependent PfMATE isomerization between OF and IF conformation is driven by protonation of a previously unidentified intracellular glutamate residue that is critical for drug resistance. Our results can be framed in a mechanistic model of transport that addresses central aspects of ligand coupling and alternating access.

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13

Arruda, Adriano Cleis, Mauro Sérgio Perilhão, Warley Almeida Santos, Marcos Fernandes Gregnani, Alexandre Budu, José Cesar Rosa Neto, Gabriel Rufino Estrela, and Ronaldo Carvalho Araujo. "PPARα-Dependent Modulation by Metformin of the Expression of OCT-2 and MATE-1 in the Kidney of Mice." Molecules 25, no. 2 (January 17, 2020): 392. http://dx.doi.org/10.3390/molecules25020392.

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Metformin is the first-line drug for type 2 diabetes mellitus control. It is established that this drug traffics through OCT-2 and MATE-1 transporters in kidney tubular cells and is excreted in its unaltered form in the urine. Hereby, we provide evidence that points towards the metformin-dependent upregulation of OCT-2 and MATE-1 in the kidney via the transcription factor proliferator-activated receptor alpha (PPARα). Treatment of wild type mice with metformin led to the upregulation of the expression of OCT-2 and MATE-1 by 34% and 157%, respectively. An analysis in a kidney tubular cell line revealed that metformin upregulated PPARα and OCT-2 expression by 37% and 299% respectively. MK-886, a PPARα antagonist, abrogated the OCT-2 upregulation by metformin and reduced MATE-1 expression. Conversely, gemfibrozil, an agonist of PPARα, elicited the increase of PPARα, OCT-2, and MATE-1 expression by 115%, 144%, and 376%, respectively. PPARα knockout mice failed to upregulate both the expression of OCT-2 and MATE-1 in the kidney upon metformin treatment, supporting the PPARα-dependent metformin upregulation of the transporters in this organ. Taken together, our data sheds light on the metformin-induced mechanism of transporter modulation in the kidney, via PPARα, and this effect may have implications for drug safety and efficacy.

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14

Claxton, Derek P., Kevin L. Jagessar, P. Ryan Steed, Richard A. Stein, and Hassane S. Mchaourab. "Sodium and proton coupling in the conformational cycle of a MATE antiporter from Vibrio cholerae." Proceedings of the National Academy of Sciences 115, no. 27 (June 18, 2018): E6182—E6190. http://dx.doi.org/10.1073/pnas.1802417115.

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Secondary active transporters belonging to the multidrug and toxic compound extrusion (MATE) family harness the potential energy of electrochemical ion gradients to export a broad spectrum of cytotoxic compounds, thus contributing to multidrug resistance. The current mechanistic understanding of ion-coupled substrate transport has been informed by a limited set of MATE transporter crystal structures from multiple organisms that capture a 12-transmembrane helix topology adopting similar outward-facing conformations. Although these structures mapped conserved residues important for function, the mechanistic role of these residues in shaping the conformational cycle has not been investigated. Here, we use double-electron electron resonance (DEER) spectroscopy to explore ligand-dependent conformational changes of NorM from Vibrio cholerae (NorM-Vc), a MATE transporter proposed to be coupled to both Na+ and H+ gradients. Distance measurements between spin labels on the periplasmic side of NorM-Vc identified unique structural intermediates induced by binding of Na+, H+, or the substrate doxorubicin. The Na+- and H+-dependent intermediates were associated with distinct conformations of TM1. Site-directed mutagenesis of conserved residues revealed that Na+- and H+-driven conformational changes are facilitated by a network of polar residues in the N-terminal domain cavity, whereas conserved carboxylates buried in the C-terminal domain are critical for stabilizing the drug-bound state. Interpreted in conjunction with doxorubicin binding of mutant NorM-Vc and cell toxicity assays, these results establish the role of ion-coupled conformational dynamics in the functional cycle and implicate H+ in the doxorubicin release mechanism.

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15

Lu, M., J. Symersky, M. Radchenko, A. Koide, Y. Guo, R. Nie, and S. Koide. "Structures of a Na+-coupled, substrate-bound MATE multidrug transporter." Proceedings of the National Academy of Sciences 110, no. 6 (January 22, 2013): 2099–104. http://dx.doi.org/10.1073/pnas.1219901110.

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16

Krah, Alexander, Roland G. Huber, Ulrich Zachariae, and Peter J. Bond. "On the ion coupling mechanism of the MATE transporter ClbM." Biochimica et Biophysica Acta (BBA) - Biomembranes 1862, no. 2 (February 2020): 183137. http://dx.doi.org/10.1016/j.bbamem.2019.183137.

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17

Burko, Yogev, Yosef Geva, Aya Refael-Cohen, Sharona Shleizer-Burko, Eilon Shani, Yael Berger, Eyal Halon, George Chuck, Menachem Moshelion, and Naomi Ori. "From Organelle to Organ: ZRIZI MATE-Type Transporter is an Organelle Transporter that Enhances Organ Initiation." Plant and Cell Physiology 52, no. 3 (January 20, 2011): 518–27. http://dx.doi.org/10.1093/pcp/pcr007.

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18

Gu, Yi-Zhong, Xiaoyan Chu, Robert Houle, Katerina Vlasakova, Kenneth A. Koeplinger, Isabelle Bourgeois, Kiran Palyada, et al. "Polyethlyene Glycol 200 Can Protect Rats Against Drug-Induced Kidney Toxicity Through Inhibition of the Renal Organic Anion Transporter 3." Toxicological Sciences 172, no. 1 (August 12, 2019): 155–66. http://dx.doi.org/10.1093/toxsci/kfz186.

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Abstract MK-7680, a cyclic nucleotide prodrug, caused significant kidney tubule injury in female rats when administered orally at 1000 mg/kg/day for 2 weeks using 10% Polysorbate 80 as vehicle. However, kidney injury was absent when MK-7680 was administered at the same dose regimen using 100% Polyethylene Glycol 200 (PEG 200) as the vehicle. Subsequent investigations revealed that MK-7680 triphosphate concentrations in kidney were much lower in rats treated with MK-7680 using PEG 200 compared with 10% Polysorbate 80 vehicle, whereas plasma exposures of MK-7680 prodrug were similar. In vitro studies demonstrated that PEG 200 is an inhibitor of human renal uptake transporter organic anion transporter 3 (OAT3), of which MK-7680 is a substrate. Furthermore, PEG 200 and PEG 400 were found to interfere in vitro with human renal transporters OAT3, organic cation transporter (OCT) 2, multidrug resistance-associated protein (MRP) 2 and 4, and multidrug and toxin extrusion protein (MATE) 1 and 2K, but not OAT1. These results support a conclusion that PEG 200 may prevent MK-7680-induced kidney injury by inhibiting its active uptake into proximal tubular cells by OAT3. Caution should be exercised therefore when using PEGs as vehicles for toxicity assessment for compounds that are substrates of renal transporters.

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Sun, Xinli, Eleanor M. Gilroy, Andrea Chini, Pedro L. Nurmberg, Ingo Hein, Christophe Lacomme, Paul R. J. Birch, Adil Hussain, Byung-Wook Yun, and Gary J. Loake. "ADS1 encodes a MATE-transporter that negatively regulates plant disease resistance." New Phytologist 192, no. 2 (July 15, 2011): 471–82. http://dx.doi.org/10.1111/j.1469-8137.2011.03820.x.

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Lu, Min, Martha Radchenko, Jindrich Symersky, Rongxin Nie, and Yi Guo. "Structural insights into H+-coupled multidrug extrusion by a MATE transporter." Nature Structural & Molecular Biology 20, no. 11 (October 20, 2013): 1310–17. http://dx.doi.org/10.1038/nsmb.2687.

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Miyamae, Shin, Ohmi Ueda, Fuminobu Yoshimura, Jaiweon Hwang, Yoshinobu Tanaka, and Hiroshi Nikaido. "A MATE Family Multidrug Efflux Transporter Pumps out Fluoroquinolones in Bacteroides thetaiotaomicron." Antimicrobial Agents and Chemotherapy 45, no. 12 (December 1, 2001): 3341–46. http://dx.doi.org/10.1128/aac.45.12.3341-3346.2001.

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ABSTRACT We cloned a gene, bexA, that codes for a multidrug efflux transporter from the chromosomal DNA of Bacteroides thetaiotaomicron ATCC 29741 by using an Escherichia coli ΔacrAB ΔacrEF mutant as a host. Although the initial recombinant construct contained other open reading frames, the presence of bexA alone was sufficient to confer to the E. coli host elevated levels of resistance to norfloxacin, ciprofloxacin, and ethidium bromide. Disruption of bexA in B. thetaiotaomicronmade the strain more susceptible to norfloxacin, ciprofloxacin, and ethidium bromide, showing that this gene is expressed in this organism and functions as a multidrug efflux pump. The deduced BexA protein sequence was homologous to the protein sequence of Vibrio parahaemolyticus NorM, a multidrug efflux transporter, and thus, BexA belongs to the multidrug and toxic compound extrusion (MATE) family.

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Ficici, Emel, Wenchang Zhou, Steven Castellano, and José D. Faraldo-Gómez. "Broadly conserved Na+-binding site in the N-lobe of prokaryotic multidrug MATE transporters." Proceedings of the National Academy of Sciences 115, no. 27 (June 18, 2018): E6172—E6181. http://dx.doi.org/10.1073/pnas.1802080115.

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Multidrug and toxic-compound extrusion (MATE) proteins comprise an important but largely uncharacterized family of secondary-active transporters. In both eukaryotes and prokaryotes, these transporters protect the cell by catalyzing the efflux of a broad range of cytotoxic compounds, including human-made antibiotics and anticancer drugs. MATEs are thus potential pharmacological targets against drug-resistant pathogenic bacteria and tumor cells. The activity of MATEs is powered by transmembrane electrochemical ion gradients, but their molecular mechanism and ion specificity are not understood, in part because high-quality structural information is limited. Here, we use computational methods to study PfMATE, from Pyrococcus furiosus, whose structure is the best resolved to date. Analysis of available crystallographic data and additional molecular dynamics simulations unequivocally reveal an occupied Na+-binding site in the N-lobe of this transporter, which had not been previously recognized. We find this site to be selective against K+ and broadly conserved among prokaryotic MATEs, including homologs known to be Na+-dependent such as NorM-VC, VmrA, and ClbM, for which the location of the Na+ site had been debated. We note, however, that the chemical makeup of the proposed Na+ site indicates it is weakly specific against H+, explaining why MATEs featuring this Na+-binding motif may be solely driven by H+ in laboratory conditions. We further posit that the concurrent coupling to H+ and Na+ gradients observed for some Na+-driven MATEs owes to a second H+-binding site, within the C-lobe. In summary, our study provides insights into the structural basis for the complex ion dependency of MATE transporters.

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Yang, Hong, Shiwei Zhou, Dong Guo, Obinna N. Obianom, Qing Li, and Yan Shu. "Divergent Regulation of OCT and MATE Drug Transporters by Cadmium Exposure." Pharmaceutics 13, no. 4 (April 13, 2021): 537. http://dx.doi.org/10.3390/pharmaceutics13040537.

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Coordinated transcellular transport by the uptake via organic cation transporters (OCTs) in concert with the efflux via multidrug and toxin extrusion proteins (MATEs) is an essential system for hepatic and renal drug disposition. Despite their clinical importance, the regulation of OCTs and MATEs remains poorly characterized. It has been reported that cadmium (Cd2+) increase the activities of OCTs while being a substrate of MATEs. Here, we found that human (h) OCT2 protein, as compared with hMATE1, was more active in trafficking between the plasma membrane and cytoplasmic storage pool. Cd2+ exposure could significantly enhance the translocation of hOCT2 and hOCT1, but not hMATE1, to the plasma membrane. We further identified that candesartan, a widely prescribed angiotensin II receptor blocker, behaved similarly toward OCT2 and MATE1 as Cd2+ did. Importantly, Cd2+ and candesartan treatments could lead to an enhanced accumulation of metformin, which is a well-characterized substrate of OCTs/MATEs, in mouse kidney and liver, respectively. Altogether, our studies have uncovered possible divergent regulation of OCTs and MATEs by certain xenobiotics, such as Cd2+ and candesartan due to the different cellular trafficking of these two families of transporter proteins, which might significantly affect drug disposition in the liver and kidney.

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Yokosho, Kengo, Naoki Yamaji, and Jian Feng Ma. "Isolation and characterisation of two MATE genes in rye." Functional Plant Biology 37, no. 4 (2010): 296. http://dx.doi.org/10.1071/fp09265.

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Multidrug and toxic compound extrusion (MATE) proteins are widely present in bacteria, fungi, plants and mammals. Recent studies have showed that a group of plant MATE genes encodes citrate transporter, which are involved in the detoxification of aluminium or translocation of iron from the roots to the shoots. In this study, we isolated two homologous genes (ScFRDL1 and ScFRDL2) from this family in rye (Secale cereale L.). ScFRDL1 shared 94.2% identity with HvAACT1, an Al-activated citrate transporter in barley (Hordeum vulgare L.) and ScFRDL2 shared 80.6% identity with OsFRDL2, a putative Al-responsive protein in rice (Oryza sativa L.). Both genes were mainly expressed in the roots, however, they showed different expression patterns. Expression of ScFRDL1 was unaffected by Al treatment, but up-regulated by Fe-deficiency treatment. In contrast, expression of ScFRDL2 was greatly induced by Al but not by Fe deficiency. The Al-induced up-regulation of ScFRDL2 was found in both the root tips and basal roots. Furthermore, the expression pattern of ScFRDL2 was consistent with citrate secretion pattern. Immunostaining showed that ScFRDL1 was localised at all cells in the root tips and central cylinder and endodermis in the basal root. Taken together, our results suggest that ScFRDL1 was involved in efflux of citrate into the xylem for Fe translocation from the roots to the shoots, while ScFRDL2 was involved in Al-activated citrate secretion in rye.

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Kusakizako, Tsukasa, Derek P. Claxton, Yoshiki Tanaka, Andrés D. Maturana, Teruo Kuroda, Ryuichiro Ishitani, Hassane S. Mchaourab, and Osamu Nureki. "Structural Basis of H+-Dependent Conformational Change in a Bacterial MATE Transporter." Structure 27, no. 2 (February 2019): 293–301. http://dx.doi.org/10.1016/j.str.2018.10.004.

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Krah, Alexander, and Ulrich Zachariae. "Insights into the ion-coupling mechanism in the MATE transporter NorM-VC." Physical Biology 14, no. 4 (June 29, 2017): 045009. http://dx.doi.org/10.1088/1478-3975/aa5ee7.

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Tanaka, Yoshiki, Christopher J. Hipolito, Andrés D. Maturana, Koichi Ito, Teruo Kuroda, Takashi Higuchi, Takayuki Katoh, et al. "Structural basis for the drug extrusion mechanism by a MATE multidrug transporter." Nature 496, no. 7444 (March 27, 2013): 247–51. http://dx.doi.org/10.1038/nature12014.

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Eisinger, Martin Lorenz, Laiyin Nie, Aline Ricarda Dörrbaum, Julian David Langer, and Hartmut Michel. "The Xenobiotic Extrusion Mechanism of the MATE Transporter NorM_PS from Pseudomonas stutzeri." Journal of Molecular Biology 430, no. 9 (April 2018): 1311–23. http://dx.doi.org/10.1016/j.jmb.2018.03.012.

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Bleasby, Kelly, Robert Houle, Michael Hafey, Meihong Lin, Jingjing Guo, Bing Lu, Rosa I. Sanchez, and Kerry L. Fillgrove. "Islatravir Is Not Expected to Be a Victim or Perpetrator of Drug-Drug Interactions via Major Drug-Metabolizing Enzymes or Transporters." Viruses 13, no. 8 (August 7, 2021): 1566. http://dx.doi.org/10.3390/v13081566.

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Islatravir (MK-8591) is a nucleoside reverse transcriptase translocation inhibitor in development for the treatment and prevention of HIV-1. The potential for islatravir to interact with commonly co-prescribed medications was studied in vitro. Elimination of islatravir is expected to be balanced between adenosine deaminase–mediated metabolism and renal excretion. Islatravir did not inhibit uridine diphosphate glucuronosyltransferase 1A1 or cytochrome p450 (CYP) enzymes CYP1A2, 2B6, 2C8, 2C9, 2C19, 2D6, or 3A4, nor did it induce CYP1A2, 2B6, or 3A4. Islatravir did not inhibit hepatic transporters organic anion transporting polypeptide (OATP) 1B1, OATP1B3, organic cation transporter (OCT) 1, bile salt export pump (BSEP), multidrug resistance-associated protein (MRP) 2, MRP3, or MRP4. Islatravir was neither a substrate nor a significant inhibitor of renal transporters organic anion transporter (OAT) 1, OAT3, OCT2, multidrug and toxin extrusion protein (MATE) 1, or MATE2K. Islatravir did not significantly inhibit P-glycoprotein and breast cancer resistance protein (BCRP); however, it was a substrate of BCRP, which is not expected to be of clinical significance. These findings suggest islatravir is unlikely to be the victim or perpetrator of drug-drug interactions with commonly co-prescribed medications, including statins, diuretics, anti-diabetic drugs, proton pump inhibitors, anticoagulants, benzodiazepines, and selective serotonin reuptake inhibitors.

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Tegli, Stefania, Lorenzo Bini, Silvia Calamai, Matteo Cerboneschi, and Carola Biancalani. "A MATE Transporter is Involved in Pathogenicity and IAA Homeostasis in the Hyperplastic Plant Pathogen Pseudomonas savastanoi pv. nerii." Microorganisms 8, no. 2 (January 22, 2020): 156. http://dx.doi.org/10.3390/microorganisms8020156.

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During the last years, many evidences have been accumulating about the phytohormone indole-3-acetic acid (IAA) as a multifaceted compound in the microbial world, with IAA playing a role as a bacterial intra and intercellular signaling molecule or as an effector during pathogenic or beneficial plant–bacteria interactions. However, pretty much nothing is known on the mechanisms that bacteria use to modulate IAA homeostasis, in particular on IAA active transport systems. Here, by an approach combining in silico three-dimensional (3D) structural modeling and docking, mutagenesis, quantitative gene expression analysis, and HPLC FLD auxin quantitative detection, for the first time a bacterial multidrug and toxic compound extrusion (MATE) transporter was demonstrated to be involved in the efflux of IAA, as well as of its conjugate IAA–Lysine, in the plant pathogenic hyperplastic bacterium Pseudomonas savastanoi pv. nerii strain Psn23. Furthermore, according to the role proved to be played by Psn23 MatE in the development of plant disease, and to the presence of Psn23 MatE homologs in all the genomospecies of the P. syringae complex, this membrane transporter could likely represent a promising target for the design of novel and selective anti-infective molecules for plant disease control.

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Jin, Sojeong, Sowon Lee, Ji-Hyeon Jeon, Hyuna Kim, Min-Koo Choi, and Im-Sook Song. "Enhanced Intestinal Permeability and Plasma Concentration of Metformin in Rats by the Repeated Administration of Red Ginseng Extract." Pharmaceutics 11, no. 4 (April 18, 2019): 189. http://dx.doi.org/10.3390/pharmaceutics11040189.

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We aimed to assess the potential herb–drug interactions between Korean red ginseng extract (RGE) and metformin in rats in terms of the modulation of metformin transporters, such as organic cation transporter (Oct), multiple toxin and extrusion protein (Mate), and plasma membrane monoamine transporter (Pmat). Single treatment of RGE did not inhibit the in vitro transport activity of OCT1/2 up to 500 µg/mL and inhibited MATE1/2-K with high IC50 value (more than 147.8 µg/mL), suggesting that concomitant used of RGE did not directly inhibit OCT- and MATE-mediated metformin uptake. However, 1-week repeated administration of RGE (1.5 g/kg/day) (1WRA) to rats showed different alterations in mRNA levels of Oct1 depending on the tissue type. RGE increased intestinal Oct1 but decreased hepatic Oct1. However, neither renal Oct1/Oct2 nor Mate1/Pmat expression in duodenum, jejunum, ileum, liver, and kidney were changed in 1WRA rats. RGE repeated dose also increased the intestinal permeability of metformin; however, the permeability of 3-O-methyl-d-glucose and Lucifer yellow was not changed in 1WRA rats, suggesting that the increased permeability of metformin by multiple doses of RGE is substrate-specific. On pharmacokinetic analysis, plasma metformin concentrations following intravenous injection were not changed in 1WRA, consistent with no significant change in renal Oct1, Oct2, and mate1. Repeated doses of RGE for 1 week significantly increased the plasma concentration of metformin, with increased half-life and urinary excretion of metformin following oral administration of metformin (50 mg/kg), which could be attributed to the increased absorption of metformin. In conclusion, repeated administration of RGE showed in vivo pharmacokinetic herb–drug interaction with metformin, with regard to its plasma exposure and increased absorption in rats. These results were consistent with increased intestinal Oct1 and its functional consequence, therefore, the combined therapeutic efficacy needs further evaluation before the combination and repeated administration of RGE and metformin, an Oct1 substrate drug.

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TANAKA, Yoshiki. "Crystal Structure Analysis of MATE, a Multidrug Efflux Transporter Leading to Multidrug Resistance." Nihon Kessho Gakkaishi 55, no. 4 (2013): 248–53. http://dx.doi.org/10.5940/jcrsj.55.248.

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33

Dridi, L., J. Tankovic, and J. C. Petit. "CdeA of Clostridium difficile, a New Multidrug Efflux Transporter of the MATE Family." Microbial Drug Resistance 10, no. 3 (September 2004): 191–96. http://dx.doi.org/10.1089/mdr.2004.10.191.

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34

Seo, Pil Joon, Jungmin Park, Mi-Jeong Park, Youn-Sung Kim, Sang-Gyu Kim, Jae-Hoon Jung, and Chung-Mo Park. "A Golgi-localized MATE transporter mediates iron homoeostasis under osmotic stress in Arabidopsis." Biochemical Journal 442, no. 3 (February 24, 2012): 551–61. http://dx.doi.org/10.1042/bj20111311.

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Iron is an essential micronutrient that acts as a cofactor in a wide variety of pivotal metabolic processes, such as the electron transport chain of respiration, photosynthesis and redox reactions, in plants. However, its overload exceeding the cellular capacity of iron binding and storage is potentially toxic to plant cells by causing oxidative stress and cell death. Consequently, plants have developed versatile mechanisms to maintain iron homoeostasis. Organismal iron content is tightly regulated at the steps of uptake, translocation and compartmentalization. Whereas iron uptake is fairly well understood at the cellular and organismal levels, intracellular and intercellular transport is only poorly understood. In the present study, we show that a MATE (multidrug and toxic compound extrusion) transporter, designated BCD1 (BUSH-AND-CHLOROTIC-DWARF 1), contributes to iron homoeostasis during stress responses and senescence in Arabidopsis. The BCD1 gene is induced by excessive iron, but repressed by iron deficiency. It is also induced by cellular and tissue damage occurring under osmotic stress. The activation-tagged mutant bcd1-1D exhibits leaf chlorosis, a typical symptom of iron deficiency. The chlorotic lesion of the mutant was partially recovered by iron feeding. Whereas the bcd1-1D mutant accumulated a lower amount of iron, the iron level was elevated in the knockout mutant bcd1-1. The BCD1 protein is localized to the Golgi complex. We propose that the BCD1 transporter plays a role in sustaining iron homoeostasis by reallocating excess iron released from stress-induced cellular damage.

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Nishima, Wataru, Yoshiki Tanaka, Ryuichiro Ishitani, Osamu Nureki, and Yuji Sugita. "Drug Extrusion Process of Mate Multidrug Efflux Transporter Revealed by Molecular Dynamics Simulations." Biophysical Journal 106, no. 2 (January 2014): 801a. http://dx.doi.org/10.1016/j.bpj.2013.11.4392.

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36

NUREKI, Osamu. "Structural Basis for the Drug Extrusion Mechanism by a MATE Multidrug Transporter and Peptide Drug Development." KAGAKU TO SEIBUTSU 52, no. 11 (2014): 725–30. http://dx.doi.org/10.1271/kagakutoseibutsu.52.725.

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37

Yang, Ye, Sarah E. Tomkovich, Marcus Mühlbauer, Xiaolun Sun, Jarrod Mousa, Ayaka Shima, Eric Oswald, Steven Bruner, and Christian Jobin. "Sa1786 Escherichia coli clbM Encodes A MATE Transporter Implicated in Colibactin Transport and Activity." Gastroenterology 150, no. 4 (April 2016): S366. http://dx.doi.org/10.1016/s0016-5085(16)31286-0.

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38

Wu, Xinxin, Ren Li, Jin Shi, Jinfang Wang, Qianqian Sun, Haijun Zhang, Yanxia Xing, Yan Qi, Na Zhang, and Yang-Dong Guo. "Brassica oleracea MATE Encodes a Citrate Transporter and Enhances Aluminum Tolerance in Arabidopsis thaliana." Plant and Cell Physiology 55, no. 8 (May 20, 2014): 1426–36. http://dx.doi.org/10.1093/pcp/pcu067.

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39

Tanaka, Yoshiki, Christopher J. Hipolito, Andrés D. Maturana, Koichi Ito, Teruo Kuroda, Takashi Higuchi, Takayuki Katoh, et al. "Author Correction: Structural basis for the drug extrusion mechanism by a MATE multidrug transporter." Nature 578, no. 7794 (January 30, 2020): E19. http://dx.doi.org/10.1038/s41586-019-1762-6.

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40

Das, Natasha, Surajit Bhattacharya, Somnath Bhattacharyya, and Mrinal K. Maiti. "Expression of rice MATE family transporter OsMATE2 modulates arsenic accumulation in tobacco and rice." Plant Molecular Biology 98, no. 1-2 (August 18, 2018): 101–20. http://dx.doi.org/10.1007/s11103-018-0766-1.

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41

Rendic, Slobodan, and Frederick Peter Guengerich. "Metabolism and Interactions of Chloroquine and Hydroxychloroquine with Human Cytochrome P450 Enzymes and Drug Transporters." Current Drug Metabolism 21, no. 14 (December 30, 2020): 1127–35. http://dx.doi.org/10.2174/1389200221999201208211537.

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Background:: In clinical practice, chloroquine and hydroxychloroquine are often co-administered with other drugs in the treatment of malaria, chronic inflammatory diseases, and COVID-19. Therefore, their metabolic properties and the effects on the activity of cytochrome P450 (P450, CYP) enzymes and drug transporters should be considered when developing the most efficient treatments for patients. Methods:: Scientific literature on the interactions of chloroquine and hydroxychloroquine with human P450 enzymes and drug transporters, was searched using PUBMED.Gov (https://pubmed.ncbi.nlm.nih.gov/) and the ADME database (https://life-science.kyushu.fujitsu.com/admedb/). Results:: Chloroquine and hydroxychloroquine are metabolized by P450 1A2, 2C8, 2C19, 2D6, and 3A4/5 in vitro and by P450s 2C8 and 3A4/5 in vivo by N-deethylation. Chloroquine effectively inhibited P450 2D6 in vitro; however, in vivo inhibition was not apparent except in individuals with limited P450 2D6 activity. Chloroquine is both an inhibitor and inducer of the transporter MRP1 and is also a substrate of the Mate and MRP1 transport systems. Hydroxychloroquine also inhibited P450 2D6 and the transporter OATP1A2. Conclusions:: Chloroquine caused a statistically significant decrease in P450 2D6 activity in vitro and in vivo, also inhibiting its own metabolism by the enzyme. The inhibition indicates a potential for clinical drug-drug interactions when taken with other drugs that are predominant substrates of the P450 2D6. When chloroquine and hydroxychloroquine are used clinically with other drugs, substrates of P450 2D6 enzyme, attention should be given to substrate-specific metabolism by P450 2D6 alleles present in individuals taking the drugs.

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Martínez-Guerrero, L. J., K. K. Evans, W. H. Dantzler, and S. H. Wright. "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 310, no. 1 (January 1, 2016): F57—F67. http://dx.doi.org/10.1152/ajprenal.00318.2015.

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Secretion of organic cations (OCs) across renal proximal tubules (RPTs) involves basolateral OC transporter (OCT)2-mediated uptake from the blood followed by apical multidrug and toxin extruder (MATE)1/2-mediated efflux into the tubule filtrate. Whereas OCT2 supports electrogenic OC uniport, MATE is an OC/H+ exchanger. As assessed by epifluorescence microscopy, cultured Chinese hamster ovary (CHO) cells that stably expressed human MATE1 accumulated the fluorescent OC N, N, N-trimethyl-2-[methyl(7-nitrobenzo[c][l,2,5]oxadiazol-4-yl)amino]ethanaminium (NBD-MTMA) in the cytoplasm and in a smaller, punctate compartment; accumulation in human OCT2-expressing cells was largely restricted to the cytoplasm. A second intracellular compartment was also evident in the multicompartmental kinetics of efflux of the prototypic OC [3H]1-methyl-4-phenylpyridinium (MPP) from MATE1-expressing CHO cells. Punctate accumulation of NBD-MTMA was markedly reduced by coexposure of MATE1-expressing cells with 5 μM bafilomycin (BAF), an inhibitor of V-type H+-ATPase, and accumulation of [3H]MPP and [3H]NBD-MTMA was reduced by >30% by coexposure with 5 μM BAF. BAF had no effect on the initial rate of MATE1-mediated uptake of NBD-MTMA, suggesting that the influence of BAF was a secondary effect involving inhibition of V-type H+-ATPase. The accumulation of [3H]MPP by isolated single nonperfused rabbit RPTs was also reduced >30% by coexposure to 5 μM BAF, suggesting that the native expression in RPTs of MATE protein within endosomes can increase steady-state OC accumulation. However, the rate of [3H]MPP secretion by isolated single perfused rabbit RPTs was not affected by 5 μM BAF, suggesting that vesicles loaded with OCs+ are not likely to recycle into the apical plasma membrane at a rate sufficient to provide a parallel pathway for OC secretion.

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Dridi, L., J. Tankovic, and J. C. Petit. "CdeA of Clostridium difficile, a New Multidrug Efflux Transporter of the MATE Family." Microbial Drug Resistance 10, no. 3 (September 1, 2004): 191–96. http://dx.doi.org/10.1089/1076629041939391.

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Nishima, Wataru, Wataru Mizukami, Yoshiki Tanaka, Ryuichiro Ishitani, Osamu Nureki, and Yuji Sugita. "Mechanisms for Two-Step Proton Transfer Reactions in the Outward-Facing Form of MATE Transporter." Biophysical Journal 110, no. 6 (March 2016): 1346–54. http://dx.doi.org/10.1016/j.bpj.2016.01.027.

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Wang, Zhenyu, Chongzhen Qian, Xiaochun Guo, Erlong Liu, Kaili Mao, Changjun Mu, Ni Chen, Wei Zhang, and Heng Liu. "ELS1, a novel MATE transporter related to leaf senescence and iron homeostasis in Arabidopsis thaliana." Biochemical and Biophysical Research Communications 476, no. 4 (August 2016): 319–25. http://dx.doi.org/10.1016/j.bbrc.2016.05.121.

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Mousa, Jarrod J., Rachel C. Newsome, Ye Yang, Christian Jobin, and Steven D. Bruner. "ClbM is a versatile, cation-promiscuous MATE transporter found in the colibactin biosynthetic gene cluster." Biochemical and Biophysical Research Communications 482, no. 4 (January 2017): 1233–39. http://dx.doi.org/10.1016/j.bbrc.2016.12.018.

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47

Tanaka, Yoshiki, Shigehiro Iwaki, Akira Sasaki, and Tomoya Tsukazaki. "Crystal structures of a nicotine MATE transporter provide insight into its mechanism of substrate transport." FEBS Letters 595, no. 14 (June 16, 2021): 1902–13. http://dx.doi.org/10.1002/1873-3468.14136.

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48

Long, Feng, Corinne Rouquette-Loughlin, William M. Shafer, and Edward W. Yu. "Functional Cloning and Characterization of the Multidrug Efflux Pumps NorM from Neisseria gonorrhoeae and YdhE from Escherichia coli." Antimicrobial Agents and Chemotherapy 52, no. 9 (June 30, 2008): 3052–60. http://dx.doi.org/10.1128/aac.00475-08.

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ABSTRACT Active efflux of antimicrobial agents is one of the most important adapted strategies that bacteria use to defend against antimicrobial factors that are present in their environment. The NorM protein of Neisseria gonorrhoeae and the YdhE protein of Escherichia coli have been proposed to be multidrug efflux pumps that belong to the multidrug and toxic compound extrusion (MATE) family. In order to determine their antimicrobial export capabilities, we cloned, expressed, and purified these two efflux proteins and characterized their functions both in vivo and in vitro. E. coli strains expressing norM or ydhE showed elevated (twofold or greater) resistance to several antimicrobial agents, including fluoroquinolones, ethidium bromide, rhodamine 6G, acriflavine, crystal violet, berberine, doxorubicin, novobiocin, enoxacin, and tetraphenylphosphonium chloride. When they were expressed in E. coli, both transporters reduced the levels of ethidium bromide and norfloxacin accumulation through a mechanism requiring the proton motive force, and direct measurements of efflux confirmed that NorM behaves as an Na+-dependent transporter. The capacities of NorM and YdhE to recognize structurally divergent compounds were confirmed by steady-state fluorescence polarization assays, and the results revealed that these transporters bind to antimicrobials with dissociation constants in the micromolar region.

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Hiasa, Miki, Takuya Matsumoto, Toshinori Komatsu, and Yoshinori Moriyama. "Wide variety of locations for rodent MATE1, a transporter protein that mediates the final excretion step for toxic organic cations." American Journal of Physiology-Cell Physiology 291, no. 4 (October 2006): C678—C686. http://dx.doi.org/10.1152/ajpcell.00090.2006.

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MATE1 was the first mammalian example of the multidrug and toxin extrusion (MATE) protein family to be identified. Human MATE1 (hMATE1) is predominantly expressed and localized to the luminal membranes of the urinary tubules and bile canaliculi and mediates H+-coupled electroneutral excretion of toxic organic cations (OCs) into urine and bile (Otsuka M, Matsumoto T, Morimoto R, Arioka S, Omote H, and Moriyama Y. Proc Natl Acad Sci USA 102: 17923–17928, 2005). mMATE1, a mouse MATE ortholog, is also predominantly expressed in kidney and liver, although its transport properties are not yet characterized. In the present study, we investigated the transport properties and localization of mMATE1. Upon expression of this protein in HEK-293 cells, mMATE1 mediated electroneutral H+/tetraethylammonium exchange and showed a substrate specificity similar to that of hMATE1. Immunological techniques with specific antibodies against mMATE1 combined with RT-PCR revealed that mMATE1 is also expressed in various cells, including brain glia-like cells and capillaries, pancreatic duct cells, urinary bladder epithelium, adrenal gland cortex, α cells of the islets of Langerhans, Leydig cells, and vitamin A-storing Ito cells. These results indicate that mMATE1 is a polyspecific H+/OC exchanger. The unexpectedly wide distribution of mMATE1 suggests involvement of this transporter protein in diverse biological functions other than excretion of OCs from the body.

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Suzuki, Masaharu, Yutaka Sato, Shan Wu, Byung-Ho Kang, and Donald R. McCarty. "Conserved Functions of the MATE Transporter BIG EMBRYO1 in Regulation of Lateral Organ Size and Initiation Rate." Plant Cell 27, no. 8 (August 2015): 2288–300. http://dx.doi.org/10.1105/tpc.15.00290.

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