Molecular properties of the SLC13 family of dicarboxylate and sulfate transporters

@article{Pajor2005MolecularPO,
  title={Molecular properties of the SLC13 family of dicarboxylate and sulfate transporters},
  author={Ana M. Pajor},
  journal={Pfl{\"u}gers Archiv},
  year={2005},
  volume={451},
  pages={597-605}
}
  • A. Pajor
  • Published 1 February 2006
  • Biology
  • Pflügers Archiv
The SLC13 gene family consists of five members in humans, with corresponding orthologs from different vertebrate species. All five genes code for sodium-coupled transporters that are found on the plasma membrane. Two of the transporters, NaS1 and NaS2, carry substrates such as sulfate, selenate and thiosulfate. The other members of the family (NaDC1, NaDC3, and NaCT) are transporters for di- and tri-carboxylates including succinate, citrate and α-ketoglutarate. The SLC13 transporters from… 
Sodium-coupled dicarboxylate and citrate transporters from the SLC13 family
  • A. Pajor
  • Biology
    Pflügers Archiv - European Journal of Physiology
  • 2013
TLDR
This review summarizes current knowledge of the structure, function, and regulation of the di- and tricarboxylate transporters of the SLC13 family and provides a new framework for understanding the mechanism of transport in this family.
Sodium-sulfate/carboxylate cotransporters (SLC13).
Molecular characteristics of transporters of C4-dicarboxylates and mechanism of translocation
TLDR
This review summarizes molecular characteristics of the C4-DCB transporters and describes perspective methodical approaches allowing association of peculiarities of structure with transport mechanism for individualtransporters.
Role of isoleucine-554 in lithium binding by the Na+/dicarboxylate cotransporter NaDC1.
TLDR
It is concluded that TM11 is likely to be an outer helix in NaDC1 that contains several residues critical for transport and Ile-554 in the middle of the helix may be an important determinant of cation affinity and selectivity.
Membrane topology structure of human high‐affinity, sodium‐dependent dicarboxylate transporter
TLDR
Results support the topography of 11 transmembrane domains with an extracellular C terminus and an intracellular N terminus of Na DC3, and for the first time provide experimental evidence for a novel topological model for NaDC3.
Sodium-dependent Extracellular Accessibility of Lys-84 in the Sodium/Dicarboxylate Cotransporter*
TLDR
Results point to a new location for Lys-84 within the substrate access pore of the Na+/dicarboxylate cotransporter, either in a transmembrane helix or a reentrant loop facing a water-filled pore.
Functional Characterization of SdcF from Bacillus licheniformis, a Homolog of the SLC13 Na+/Dicarboxylate Transporters
TLDR
SdcF is a secondary active transporter for four- and five-carbon dicarboxylates that can use Na+ or Li+ as a driving cation and results support an ordered binding mechanism for SdcF in which sodium binds first and succinate binds last.
Role of Ile-554 in lithium binding by the Na + /dicarboxylate cotransporter, NaDC1 †
TLDR
It is concluded that TM 11 is likely to be an outer helix in NaDC1 that contains several residues critical for transport, including Ile-554 in the middle of the helix, which may be an important determinant of cation affinity and selectivity.
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