Sodium-coupled transporters for Krebs cycle intermediates

Annu Rev Physiol. 1999;61:663-82. doi: 10.1146/annurev.physiol.61.1.663.

Abstract

Krebs cycle intermediates such as succinate, citrate, and alpha-ketoglutarate are transferred across plasma membranes of cells by secondary active transporters that couple the downhill movement of sodium to the concentrative uptake of substrate. Several transporters have been identified in isolated membrane vesicles and cells based on their functional properties, suggesting the existence of at least three or more Na+/dicarboxylate cotransporter proteins in a given species. Recently, several cDNAs, called NaDC-1, coding for the low-affinity Na+/dicarboxylate cotransporters have been isolated from rabbit, human, and rat kidney. The Na+/dicarboxylate cotransporters are part of a distinct gene family that includes the renal and intestinal Na+/sulfate cotransporters. Other members of this family include a Na(+)- and Li(+)-dependent dicarboxylate transporter from Xenopus intestine and a putative Na+/dicarboxylate cotransporter from rat intestine. The current model of secondary structure in NaDC-1 contains 11 transmembrane domains and an extracellular N-glycosylated carboxy terminus.

Publication types

  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Animals
  • Carrier Proteins / chemistry
  • Carrier Proteins / genetics
  • Carrier Proteins / metabolism*
  • Citric Acid Cycle / physiology*
  • Cloning, Molecular
  • Dicarboxylic Acid Transporters*
  • Humans
  • Membrane Proteins / chemistry
  • Membrane Proteins / genetics
  • Membrane Proteins / metabolism
  • Organic Anion Transporters, Sodium-Dependent*
  • Sodium / metabolism*
  • Structure-Activity Relationship
  • Symporters*

Substances

  • Carrier Proteins
  • Dicarboxylic Acid Transporters
  • Membrane Proteins
  • Organic Anion Transporters, Sodium-Dependent
  • SLC13A2 protein, human
  • Slc13a2 protein, rat
  • Symporters
  • Sodium