Synergy and specificity of two Na+-aromatic amino acid symporters in the model alimentary canal of mosquito larvae

Bernard A. Okech, Ella A. Meleshkevitch, Melissa M. Miller, Lyudmila B. Popova, William R. Harvey, Dmitri Y. Boudko

Research output: Contribution to journalArticlepeer-review

20 Scopus citations


The nutrient amino acid transporter (NAT) subfamily is the largest subdivision of the sodium neurotransmitter symporter family (SNF; also known as SLC6; HUGO). There are seven members of the NAT population in the African malaria mosquito Anopheles gambiae, two of which, AgNAT6 and AgNAT8, preferably transport indole- and phenyl-branched substrates, respectively. The relative expression and distribution of these aromatic NATs were examined with transporter-specific antibodies in Xenopus oocytes and mosquito larval alimentary canal, representing heterologous and tissue expression systems, respectively. NAT-specific aromatic-substrate-induced currents strongly corresponded with specific accumulation of both transporters in the plasma membrane of oocytes. Immunolabeling revealed elevated expressions of both transporters in specific regions of the larval alimentary canal, including salivary glands, cardia, gastric caeca, posterior midgut and Malpighian tubules. Differences in relative expression densities and spatial distribution of the transporters were prominent in virtually all of these regions, suggesting unique profiles of the aromatic amino acid absorption. For the first time reversal of the location of a transporter between apical and basal membranes was identified in posterior and anterior epithelial domains corresponding with secretory and absorptive epithelial functions, respectively. Both aromatic NATs formed putative homodimers in the larval gut whereas functional monomers were over-expressed heterologously in Xenopus oocytes. The results unequivocally suggest functional synergy between substrate-specific AgNAT6 and AgNATS in intracellular absorption of aromatic amino acids. More broadly, they suggest that the specific selectivity, regional expression and polarized membrane docking of NATs represent key adaptive traits shaping functional patterns of essential amino acid absorption in the metazoan alimentary canal and other tissues.

Original languageEnglish
Pages (from-to)1594-1602
Number of pages9
JournalJournal of Experimental Biology
Issue number10
StatePublished - May 2008
Externally publishedYes


  • Anopheles gambiae
  • Co-transporter
  • Essential amino acid
  • Insect
  • Malaria
  • Monoamine neurotransmitter
  • Mosquito
  • NAT
  • Nutrient amino acid transporter
  • Phenylalanine
  • Tryptophan


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