VPS26 Moonlights as an Arrestin-like Adapter for a 7-transmembrane RGS 2 protein in Arabidopsis thaliana
Extracellular signals perceived by 7-transmembrane (7TM)-spanning receptors on the plasma membrane utilize a cytoplasmic adaptor that propagates signaling and initiates a feedback circuit for desensitization by removal of these receptors at the plasma membrane leading to desensitization to that signal. Signal (agonist) binding often evokes phosphorylation at the C-terminal tail of many 7TM G-protein-coupled receptors in animal cells which then recruits a cytoplasmic intermediate adaptor, β-arrestin, that sets in motion clathrin-mediated endocytosis (CME). Some 7TM receptors have agonist-induced phosphorylation and CME that do not involve β-arrestin, therefore it is unclear how these phosphorylated 7TM receptors are internalized. Arrestins, neither α– or β-types, are not encoded in the Arabidopsis genome, yet Arabidopsis cells have a well characterized signal-induced CME of a 7TM protein, Regulator of G Signaling 1 (AtRGS1). We show that a component of the retromer complex, VPS26, moonlights as an arrestin-like adapter. VPS26A and VPS26B form heterodimer instead of homodimer or monomer. flg22, a bacterium-derived signal that alerts plant cells of the presence of a potential pathogen, induces phosphorylation of AtRGS1 within a cluster of serines in its C-terminal tail, dimerization, and its CME. The phosphorylated C-terminal tail peptide binds to VPS26A/B heterodimer with greater affinity than the unphosphorylated peptide. We propose that VPS26 serves as an arrestin-like adaptor in the CME of AtRGS1 dimerization biased for VPS26 signaling.