Substrate specificity and transport mechanism of amino-acid transceptor Slimfast from Aedes aegypti.

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 expres

SUBMITTER: Boudko DY 

PROVIDER: S-EPMC4608377 | biostudies-literature | 2015 Oct

REPOSITORIES: biostudies-literature