A caspase-like decoy molecule enhances the activity of a paralogous caspase in the yellow fever mosquito, Aedes aegypti.

Détails

ID Serval
serval:BIB_C6F4749E915F
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
A caspase-like decoy molecule enhances the activity of a paralogous caspase in the yellow fever mosquito, Aedes aegypti.
Périodique
Insect Biochemistry and Molecular Biology
Auteur(s)
Bryant B., Ungerer M.C., Liu Q., Waterhouse R.M., Clem R.J.
ISSN
1879-0240 (Electronic)
ISSN-L
0965-1748
Statut éditorial
Publié
Date de publication
2010
Peer-reviewed
Oui
Volume
40
Numéro
7
Pages
516-523
Langue
anglais
Résumé
Caspases are cysteine proteases that play critical roles in apoptosis and other key cellular processes. A mechanism of caspase regulation that has been described in mammals and nematodes involves caspase-like decoy molecules, enzymatically inactive caspase homologs that have arisen by gene duplication and acquired the ability to regulate other caspases. Caspase-like decoy molecules are not found in Drosophila melanogaster, raising the question of whether this type of caspase regulation exists in insects. Phylogenomic analysis of caspase genes from twelve Drosophila and three mosquito species revealed several examples of duplicated caspase homologs lacking critical catalytic residues, making them candidate caspase-like decoy molecules. One of these, CASPS18 from the mosquito Aedes aegypti, is a homolog of the D. melanogaster caspase Decay and contains substitutions in two critical amino acid positions, including the catalytic cysteine residue. As expected, CASPS18 lacked caspase activity, but co-expression of CASPS18 with a paralogous caspase, CASPS19, in mosquito cells or co-incubation of CASPS18 and CASPS19 recombinant proteins resulted in greatly enhanced CASPS19 activity. The discovery of potential caspase-like decoy molecules in several insect species opens new avenues for investigating caspase regulation in insects, particularly in disease vectors such as mosquitoes.

Mots-clé
Aedes/enzymology, Amino Acid Sequence, Animals, Caspases/chemistry, Caspases/metabolism, Caspases/physiology, Conserved Sequence, Enzyme Activation, Gene Duplication, Insect Proteins/chemistry, Insect Proteins/metabolism, Insect Proteins/physiology, Phylogeny, Recombinant Fusion Proteins/metabolism, Sequence Analysis, Protein
Pubmed
Web of science
Création de la notice
20/09/2017 11:18
Dernière modification de la notice
03/03/2018 21:18
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