Author
Listed:
- Dmitri Y. Boudko
(Rosalind Franklin University)
- Hitoshi Tsujimoto
(New Mexico State University)
- Stacy D. Rodriguez
(New Mexico State University)
- Ella A. Meleshkevitch
(Rosalind Franklin University)
- David P. Price
(Molecular Biology Program, New Mexico State University)
- Lisa L. Drake
(New Mexico State University)
- Immo A. Hansen
(New Mexico State University
Molecular Biology Program, New Mexico State University
Institute for Applied Biosciences, New Mexico State University)
Abstract
Anautogenous mosquitoes depend on vertebrate blood as nutrient source for their eggs. A highly efficient set of membrane transporters mediates the massive movement of nutrient amino acids between mosquito tissues after a blood meal. Here we report the characterization of the amino-acid transporter Slimfast (Slif) from the yellow-fever mosquito Aedes aegypti using codon-optimized heterologous expression. Slif is a well-known component of the target-of-rapamycin signalling pathway and fat body nutrient sensor, but its substrate specificity and transport mechanism were unknown. We found that Slif transports essential cationic and neutral amino acids with preference for arginine. It has an unusual dual-affinity mechanism with only the high affinity being Na+ dependent. Tissue-specific expression and blood meal-dependent regulation of Slif are consistent with conveyance of essential amino acids from gut to fat body. Slif represents a novel transport system and type of transceptor for sensing and transporting essential amino acids during mosquito reproduction.
Suggested Citation
Dmitri Y. Boudko & Hitoshi Tsujimoto & Stacy D. Rodriguez & Ella A. Meleshkevitch & David P. Price & Lisa L. Drake & Immo A. Hansen, 2015.
"Substrate specificity and transport mechanism of amino-acid transceptor Slimfast from Aedes aegypti,"
Nature Communications, Nature, vol. 6(1), pages 1-10, December.
Handle:
RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms9546
DOI: 10.1038/ncomms9546
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