ArticleInsect biochemistry and molecular biology2010
A caspase-like decoy molecule enhances the activity of a paralogous caspase in the yellow fever mosquito, Aedes aegypti.
Article in Insect biochemistry and molecular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 60 citations in OpenAlex.
- Evolutionary novelty in the apoptotic pathway of aphids.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- The midgut transcriptome of Aedes aegypti fed with saline or protein meals containing chikungunya virus reveals genes potentially involved in viral midgut escape.BMC genomics · 2017Article
- Functional Validation of Apoptosis Genes IAP1 and DRONC in Midgut Tissue of the Biting Midge Culicoides sonorensis (Diptera: Ceratopogonidae) by RNAi.Journal of medical entomology · 2017Article
- The Caenorhabditis elegans matrix non-peptidase MNP-1 is required for neuronal cell migration and interacts with the Ror receptor tyrosine kinase CAM-1.Developmental biology · 2017Article
- Infection pattern and transmission potential of chikungunya virus in two New World laboratory-adapted Aedes aegypti strains.Scientific reports · 2016Article
- Induction of reaper ortholog mx in mosquito midgut cells following baculovirus infection.Cell death and differentiation · 2011Article
- A comprehensive characterization of the caspase gene family in insects from the order Lepidoptera.BMC genomics · 2011Article
- The role of IAP antagonist proteins in the core apoptosis pathway of the mosquito disease vector Aedes aegypti.Apoptosis : an international journal on programmed cell death · 2011Article
- Defining the core apoptosis pathway in the mosquito disease vector Aedes aegypti: the roles of iap1, ark, dronc, and effector caspases.Apoptosis : an international journal on programmed cell death · 2011Article
- The genomic underpinnings of apoptosis in the silkworm, Bombyx mori.BMC genomics · 2010Article
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Authors and funding
5 authors at 2 institutions in 3 countries.
Funding
Abstract
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.
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