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Mint/X11 PDZ domains from non-bilaterian animals recognize and bind CaV2 calcium channel C-termini in vitro
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Mint/X11 PDZ domains from non-bilaterian animals recognize and bind CaV2 calcium channel C-termini in vitro
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Journal Article
Mint/X11 PDZ domains from non-bilaterian animals recognize and bind CaV2 calcium channel C-termini in vitro
2024
Overview
PDZ domain mediated interactions with voltage-gated calcium (Ca
V
) channel C-termini play important roles in localizing membrane Ca
2+
signaling. The first such interaction was described between the scaffolding protein Mint-1 and Ca
V
2.2 in mammals. In this study, we show through various in silico analyses that Mint is an animal-specific gene with a highly divergent N-terminus but a strongly conserved C-terminus comprised of a phosphotyrosine binding domain, two tandem PDZ domains (PDZ-1 and PDZ-2), and a C-terminal auto-inhibitory element that binds and inhibits PDZ-1. In addition to Ca
V
2 chanels, most genes that interact with Mint are also deeply conserved including amyloid precursor proteins, presenilins, neurexin, and CASK and Veli which form a tripartite complex with Mint in bilaterians. Through yeast and bacterial 2-hybrid experiments, we show that Mint and Ca
V
2 channels from cnidarians and placozoans interact in vitro, and in situ hybridization revealed co-expression in dissociated neurons from the cnidarian
Nematostella vectensis
. Unexpectedly, the Mint orthologue from the ctenophore
Hormiphora californiensis
strongly bound the divergent C-terminal ligands of cnidarian and placozoan Ca
V
2 channels, despite neither the ctenophore Mint, nor the placozoan and cnidarian orthologues, binding the ctenophore Ca
V
2 channel C-terminus. Altogether, our analyses suggest that the capacity of Mint to bind Ca
V
2 channels predates bilaterian animals, and that evolutionary changes in Ca
V
2 channel C-terminal sequences resulted in altered binding modalities with Mint.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
/ Animals
/ Calcium channels (voltage-gated)
/ Genes
/ Humanities and Social Sciences
/ Insects
/ Ligands
/ NMR
/ Proteins
/ Science
/ Yeast
