SLC13 family of Na+-coupled di- and tri-carboxylate/sulfate transporters

Bergeron, Marc J.; Clémençon, Benjamin; Hediger, Matthias A.; Markovich, Daniel

doi:10.1016/j.mam.2012.12.001

Cited by 108 publications

(113 citation statements)

References 87 publications

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“…1 and 2) no electrogenic malateinduced currents are detectable on isolated vacuoles (Supplemental Figure 3). Interestingly, the preference of tDT from Arabidopsis to accept carboxylates in the divalent anionic form concurs with the basic transport properties of the corresponding animal specific protein SLC13 (15,16,31), being structurally the closest tDT homologous transporter. Interestingly, while tDT transports its substrates in a counter-exchange mode ( Figure 5) all other SLC13 members analysed so far are characterized to be sodium/carboxylate symporters (15,32).…”

Section: -) Formmentioning

confidence: 63%

“…While several members of the tDT homologs in animal systems, namely SLC13 proteins also transport sulphate (16) we demonstrated that tDT from Arabidopsis does not accept sulphate, nor its structurally related phosphate, as substrates ( Figure 5). This inability of tDT to accept sulphate and phosphate as substrates concurs, however, with the presence of specific PO 4 2--and SO 4 2-carriers in the vacuolar membrane (33,34).…”

Section: -) Formmentioning

confidence: 82%

“…In Arabidopsis, no homologs of the tDT gene exist and the presence of this carrier is most likely limited to the vacuolar membrane (14) and plant tDT proteins group into the so called SLC13 family. In contrast to tDT, all SLC13 proteins in animal cells reside on the plasma membrane and catalyze sodium-coupled import of various carboxylates (15,16).…”

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confidence: 99%

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Purification and functional characterization of the vacuolar malate transporter tDT from Arabidopsis

Frei

Eisenach

Martinoia

et al. 2018

Journal of Biological Chemistry

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The exact transport characteristics of the vacuolar dicarboxylate transporter tDT from Arabidopsis are elusive. To overcome this limitation, we combined a range of experimental approaches comprising generation/analysis of tDT overexpressors, 13 CO 2 feeding and quantification of 13 C enrichment, functional characterization of tDT in proteoliposomes and electrophysiological studies on vacuoles. tdt knock-out plants showed decreased malate and increased citrate concentrations in leaves during the diurnal light-dark rhythm and after onset of drought, when compared to wild types. Interestingly, under latter two conditions tDT overexpressors exhibited malate-and citrate levels opposite to tdt knock-out plants. Highly purified tDT protein transports malate and citrate in a 1:1 antiport mode. The apparent affinity for malate decreased with decreasing pH, while citrate affinity increased. This observation indicates that tDt exhibits a preference for dianion substrates, which is supported by electrophysiological analysis on intact vacuoles. tDT also accepts fumarate and succinate as substrates, but not α-ketoglutarate, gluconate, sulphate or phosphate. Taking tDT as an example we demonstrated that it is possible to reconstitute a vacuolar metabolite transporter functionally in proteoliposomes. The displayed, so far unknown counter-exchange properties of tDT now explains the frequently observed reciprocal concentration changes of malate and citrate in leaves from various plant species. tDT from Arabidopsis is the first member of the wellknown and widely present SLC13 group of carrier proteins, exhibiting an antiport mode of transport.

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Section: -) Formmentioning

confidence: 63%

Section: -) Formmentioning

confidence: 82%

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Purification and functional characterization of the vacuolar malate transporter tDT from Arabidopsis

Frei

Eisenach

Martinoia

et al. 2018

Journal of Biological Chemistry

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“…This gene family further consists of two sodium-coupled dicarboxylate transporters, NaDC1 (SLC13A2) and NaDC3 (SLC13A3), and two sodiumcoupled sulfate transporters, NaS1 (SLC13A1) and NaS2 (SLC13A4) (Markovich and Murer, 2004;Pajor, 2006Pajor, , 2014Markovich, 2012;Bergeron et al, 2013;Willmes and Birkenfeld, 2013). NaCT has been cloned from various species, including humans (Inoue et al, 2002a), rats (Inoue et al, 2002b), and mice .…”

Section: Introductionmentioning

confidence: 99%

Electrophysiological Characterization of Human and Mouse Sodium-Dependent Citrate Transporters (NaCT/SLC13A5) Reveal Species Differences with Respect to Substrate Sensitivity and Cation Dependence

Zwart

Peeva

Rong

et al. 2015

J Pharmacol Exp Ther

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The citric acid cycle intermediate citrate plays a crucial role in metabolic processes such as fatty acid synthesis, glucose metabolism, and b-oxidation. Citrate is imported from the circulation across the plasma membrane into liver cells mainly by the sodium-dependent citrate transporter (NaCT; SLC13A5). Deletion of NaCT from mice led to metabolic changes similar to caloric restriction; therefore, NaCT has been proposed as an attractive therapeutic target for the treatment of obesity and type 2 diabetes. In this study, we expressed mouse and human NaCT into Xenopus oocytes and examined some basic functional properties of those transporters. Interestingly, striking differences were found between mouse and human NaCT with respect to their sensitivities to citric acid cycle intermediates as substrates for these transporters. Mouse NaCT had at least 20-to 800-fold higher affinity for these intermediates than human NaCT. Mouse NaCT is fully active at physiologic plasma levels of citrate, but its human counterpart is not. Replacement of extracellular sodium by other monovalent cations revealed that human NaCT was markedly less dependent on extracellular sodium than mouse NaCT. The low sensitivity of human NaCT for citrate raises questions about the translatability of this target from the mouse to the human situation and raises doubts about the validity of this transporter as a therapeutic target for the treatment of metabolic diseases in humans.

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“…SLC13A5 is a sodium-coupled transporter that mediates cellular uptake of citrate, which plays important role in the synthesis of fatty acids (Li et al, 2015). Mammalian solute carrier family 13 mediates transport of Na + -coupled anion at the plasma membrane of epithelial (kidney, small intestine, placenta, and liver) (Pajor, 2006;Bergeron et al, 2013). CpG sites of SLC13A5 in glioblastomas exhibited that expression level had a negative correlation with promoter methylation (Etcheverry et al, 2010).…”

Section: Introductionmentioning

confidence: 99%

Molecular characterization, tissue expression profile, and SNP analysis of porcine SLC13A5

Wang¹,

Jiang²,

Ma³

2015

Genet. Mol. Res.

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ABSTRACT. Solute carrier family 13 (sodium-dependent citrate transporter member 5, SLC13A5) gene has been recently found to play an important role in intramuscular fat content in pigs. In this study, the full-length cDNA of porcine SLC13A5 was obtained from the longissimus dorsi muscle of Shaziling pigs, using the rapid amplification of cDNA ends technique. Full-length porcine SLC13A5 cDNA was 2118 bp, with a 1665-bp open reading frame encoding 554 amino acids. The porcine SLC13A5 protein was analyzed using bioinformatic methodology, and found to include 18 potential phosphorylation sites (including six serine, nine threonine, and three tyrosine) and eight putative transmembrane domains. One single nucleotide polymorphism (SNP) site, A251G, was identified by polymerase chain reaction (PCR)-restriction fragment (2015) length polymorphism and the associations of this SNP with age at 100 kg and corrected back fat thickness were found to be not significant. Expression of SLC13A5 was evaluated in ten tissues from 25-day-old full-sib Yorkshire and Shaziling piglets (both N = 3), using quantitative PCR analysis. Expression levels of SLC13A5 differed significantly between the breeds in cecum, liver and crureus muscle. In each breed, gene expression levels were significantly different in longissimus dorsi muscle, compared to the nine other tissues. This study has laid the foundation for further investigations of the molecular mechanisms of SLC13A5 in pigs.

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SLC13 family of Na+-coupled di- and tri-carboxylate/sulfate transporters

Cited by 108 publications

References 87 publications

Purification and functional characterization of the vacuolar malate transporter tDT from Arabidopsis

Purification and functional characterization of the vacuolar malate transporter tDT from Arabidopsis

Electrophysiological Characterization of Human and Mouse Sodium-Dependent Citrate Transporters (NaCT/SLC13A5) Reveal Species Differences with Respect to Substrate Sensitivity and Cation Dependence

Molecular characterization, tissue expression profile, and SNP analysis of porcine SLC13A5

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