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Molecular analysis of the serine/threonine kinase Akt and its expression in the mosquito Aedes aegypti
Author(s) -
Riehle M. A.,
Brown M. R.
Publication year - 2003
Publication title -
insect molecular biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.955
H-Index - 93
eISSN - 1365-2583
pISSN - 0962-1075
DOI - 10.1046/j.1365-2583.2003.00405.x
Subject(s) - biology , aedes aegypti , akt1 , akt3 , pleckstrin homology domain , protein kinase b , anopheles gambiae , threonine , akt2 , protein kinase domain , serine , kinase , gene , microbiology and biotechnology , phosphorylation , genetics , botany , larva , immunology , malaria , mutant
A key component of the insulin‐signalling pathway, the protein kinase Akt, was identified and cloned as a cDNA from ovaries of the mosquito Aedes aegypti . An ortholog gene was found in the Anopheles gambiae genome database, and like other Akts, both mosquito Akts possess pleckstrin homology domains for membrane binding and a serine/threonine kinase domain. When Ae. aegypti ovaries were treated with bovine insulin in vitro , a putative Akt was threonine‐phosphorylated, as expected for Akts. AaegAKT was only expressed in embryos for the first 6 h after oviposition and in ovaries before and during a gonotrophic cycle.