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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 L

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2

Tocci, Nadia, Francesco Iannelli, Alessandro Bidossi, et al. "Functional Analysis of Pneumococcal Drug Efflux Pumps Associates the MATE DinF Transporter with Quinolone Susceptibility." Antimicrobial Agents and Chemotherapy 57, no. 1 (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) tran

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3

Zakrzewska, Sandra, Ahmad Reza Mehdipour, Viveka Nand Malviya, et al. "Inward-facing conformation of a multidrug resistance MATE family transporter." Proceedings of the National Academy of Sciences 116, no. 25 (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 st

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4

Väisänen, Enni, Junko Takahashi, Ogonna Obudulu, et al. "Hunting monolignol transporters: membrane proteomics and biochemical transport assays with membrane vesicles of Norway spruce." Journal of Experimental Botany 71, no. 20 (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 al

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5

Kusakizako, Tsukasa, Yoshiki Tanaka, Christopher J. Hipolito, et al. "LCP crystallization and X-ray diffraction analysis of VcmN, a MATE transporter fromVibrio cholerae." Acta Crystallographica Section F Structural Biology Communications 72, no. 7 (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 grou

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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 (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 та ін. "PPAR-α Deletion Attenuates Cisplatin Nephrotoxicity by Modulating Renal Organic Transporters MATE-1 and OCT-2". International Journal of Molecular Sciences 21, № 19 (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

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8

Kusakizako, Tsukasa, Yoshiki Tanaka, Andrés Maturana, et al. "X-ray crystallographic analysis of a MATE multidrug transporter from V. cholerae." Acta Crystallographica Section A Foundations and Advances 70, a1 (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

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9

Dobritzsch, Melanie, Tilo Lübken, Lennart Eschen-Lippold, et al. "MATE Transporter-Dependent Export of Hydroxycinnamic Acid Amides." Plant Cell 28, no. 2 (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 (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

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11

Zhang, Haiwen, Fu-Geng Zhao, Ren-Jie Tang, et al. "Two tonoplast MATE proteins function as turgor-regulating chloride channels inArabidopsis." Proceedings of the National Academy of Sciences 114, no. 10 (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 bent

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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 (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 i

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13

Arruda, Adriano Cleis, Mauro Sérgio Perilhão, Warley Almeida Santos та ін. "PPARα-Dependent Modulation by Metformin of the Expression of OCT-2 and MATE-1 in the Kidney of Mice". Molecules 25, № 2 (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

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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 (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

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15

Lu, M., J. Symersky, M. Radchenko, et al. "Structures of a Na+-coupled, substrate-bound MATE multidrug transporter." Proceedings of the National Academy of Sciences 110, no. 6 (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 (2020): 183137. http://dx.doi.org/10.1016/j.bbamem.2019.183137.

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17

Burko, Yogev, Yosef Geva, Aya Refael-Cohen, et al. "From Organelle to Organ: ZRIZI MATE-Type Transporter is an Organelle Transporter that Enhances Organ Initiation." Plant and Cell Physiology 52, no. 3 (2011): 518–27. http://dx.doi.org/10.1093/pcp/pcr007.

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18

Gu, Yi-Zhong, Xiaoyan Chu, Robert Houle, 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 (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 st

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19

Sun, Xinli, Eleanor M. Gilroy, Andrea Chini, et al. "ADS1 encodes a MATE-transporter that negatively regulates plant disease resistance." New Phytologist 192, no. 2 (2011): 471–82. http://dx.doi.org/10.1111/j.1469-8137.2011.03820.x.

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20

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 (2013): 1310–17. http://dx.doi.org/10.1038/nsmb.2687.

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21

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 (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 expr

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22

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 (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, i

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23

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 (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+ ex

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24

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-

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Kusakizako, Tsukasa, Derek P. Claxton, Yoshiki Tanaka, et al. "Structural Basis of H+-Dependent Conformational Change in a Bacterial MATE Transporter." Structure 27, no. 2 (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 (2017): 045009. http://dx.doi.org/10.1088/1478-3975/aa5ee7.

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27

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

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28

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 (2018): 1311–23. http://dx.doi.org/10.1016/j.jmb.2018.03.012.

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Bleasby, Kelly, Robert Houle, Michael Hafey, et al. "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 (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 transporte

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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 (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

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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 (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

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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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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 (2004): 191–96. http://dx.doi.org/10.1089/mdr.2004.10.191.

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Seo, Pil Joon, Jungmin Park, Mi-Jeong Park, et al. "A Golgi-localized MATE transporter mediates iron homoeostasis under osmotic stress in Arabidopsis." Biochemical Journal 442, no. 3 (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 we

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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 (2014): 801a. http://dx.doi.org/10.1016/j.bpj.2013.11.4392.

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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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Yang, Ye, Sarah E. Tomkovich, Marcus Mühlbauer, et al. "Sa1786 Escherichia coli clbM Encodes A MATE Transporter Implicated in Colibactin Transport and Activity." Gastroenterology 150, no. 4 (2016): S366. http://dx.doi.org/10.1016/s0016-5085(16)31286-0.

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Wu, Xinxin, Ren Li, Jin Shi, et al. "Brassica oleracea MATE Encodes a Citrate Transporter and Enhances Aluminum Tolerance in Arabidopsis thaliana." Plant and Cell Physiology 55, no. 8 (2014): 1426–36. http://dx.doi.org/10.1093/pcp/pcu067.

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

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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 (2018): 101–20. http://dx.doi.org/10.1007/s11103-018-0766-1.

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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 (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/)

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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 (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

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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 (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 (2016): 1346–54. http://dx.doi.org/10.1016/j.bpj.2016.01.027.

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Wang, Zhenyu, Chongzhen Qian, Xiaochun Guo, et al. "ELS1, a novel MATE transporter related to leaf senescence and iron homeostasis in Arabidopsis thaliana." Biochemical and Biophysical Research Communications 476, no. 4 (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 (2017): 1233–39. http://dx.doi.org/10.1016/j.bbrc.2016.12.018.

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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 (2021): 1902–13. http://dx.doi.org/10.1002/1873-3468.14136.

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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 (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 exp

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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 (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 charac

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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 (2015): 2288–300. http://dx.doi.org/10.1105/tpc.15.00290.

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