GEPHE SUMMARY Print
cellular organisms; Eukaryota; Opisthokonta; Metazoa; Eumetazoa; Bilateria; Protostomia; Ecdysozoa; Panarthropoda; Arthropoda; Mandibulata; Pancrustacea; Hexapoda
NCBI Taxonomy ID
is Taxon A an Infraspecies?
Liriomyza asclepiadis Spencer, 1969; Liriomyza aclepiadis
Show more ... xapoda; Insecta; Dicondylia; Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha; Eremoneura; Cyclorrhapha; Schizophora; Acalyptratae; Opomyzoidea; Agromyzidae; Phytomyzinae; Liriomyza
NCBI Taxonomy ID
is Taxon B an Infraspecies?
Generic Gene Name
Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IIC subfamily.
GO - Molecular Function
GO:0005524 : ATP binding ... show more
GO - Biological Process
GO - Cellular Component
GO:0016021 : integral component of membrane ... show more
SNP Coding Change
Molecular Details of the Mutation
|Taxon A||Taxon B||Position|
Dobler S; Dalla S; Wagschal V; Agrawal AA
The extent of convergent molecular evolution is largely unknown, yet is critical to understanding the genetics of adaptation. Target site insensitivity to cardenolides is a prime candidate for studying molecular convergence because herbivores in six orders of insects have specialized on these plant poisons, which gain their toxicity by blocking an essential transmembrane carrier, the sodium pump (Na,K-ATPase). We investigated gene sequences of the Na,K-ATPase α-subunit in 18 insects feeding on cardenolide-containing plants (spanning 15 genera and four orders) to screen for amino acid substitutions that might lower sensitivity to cardenolides. The replacement N122H that was previously shown to confer resistance in the monarch butterfly (Danaus plexippus) and Chrysochus leaf beetles was found in four additional species, Oncopeltus fasciatus and Lygaeus kalmii (Heteroptera, Lygaeidae), Labidomera clivicollis (Coleoptera, Chrysomelidae), and Liriomyza asclepiadis (Diptera, Agromyzidae). Thus, across 300 Myr of insect divergence, specialization on cardenolide-containing plants resulted in molecular convergence for an adaptation likely involved in coevolution. Our screen revealed a number of other substitutions connected to cardenolide binding in mammals. We confirmed that some of the particular substitutions provide resistance to cardenolides by introducing five distinct constructs of the Drosophila melanogaster gene into susceptible eucaryotic cells under an ouabain selection regime. These functional assays demonstrate that combined substitutions of Q(111) and N(122) are synergistic, with greater than twofold higher resistance than either substitution alone and >12-fold resistance over the wild type. Thus, even across deep phylogenetic branches, evolutionary degrees of freedom seem to be limited by physiological constraints, such that the same molecular substitutions confer adaptation.
47 (ABCA2, BTR1- Cadherin-like protein, Ha_BtR, ABCC2, cadherin, para (kdr), Chitin synthase 1 (CHS1), CYP6BG1, FMO2, MAP4K4, Acetylcholinesterase (Ace-1), resistance to dieldrin, Cpm1, esterase B1, Acetylcholinesterase (Ace-2), alcohol dehydrogenase (Adh), Aldehyde dehydrogenase (Aldh), CG11699, Cyp12d1, Cyp28d1, Cyp28d1-Cyp28d2, cyp6d2, cyp6g1, GSS (glutathione synthetase), GSTE1-E10 cluster, kin of irre (kire), PHGPx, RnrS, SOD1, Ugt86Dd, Acetylcholinesterase (Ace), CYP6D1, esterase isozyme E7 = E3, esterase E4, CYP6AB3, CYP6FU1, CYP6P9 cluster (CYP6P9a and CYP6P9b), CYP6P9; CYP6P4 cluster, CYP9M10, esterase B1 + esterase A, esterase B1 = esterase beta1, esterase isozyme E3, CHKov1, CYP6B1, CYP6B4, FMO1, CYP6CY3)
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