Latrophyllins belong to the family of adhesion G protein-coupled receptors, capable of binding to actin-associated scaffold proteins. They are expressed in various tissues, suggesting that they might participate in biological processes that are ubiquitous. Here we focus on actin cytoskeleton dynamics to explore the role of latrophilins in mammalian cells. Overexpression of each latrophilin isoform comparably increased cell volume while modifying the net profile of F-actin-dependent cell structures, as evaluated by confocal microscopy analysis. Latrophilin deletion mutants evidenced that direct coupling to the intracellular machinery was a requirement for modulating cell structures. The association between latrophilins and the actin cytoskeleton was detected by co-immunoprecipitation assays and corroborated with immunocytochemistry analysis. Consistent with the destabilization of F-actin structures, latrophilin isoforms constitutively induced a prominent increase in the activity of actin depolymerizing factor, cofilin, evaluated by western blot assays. Intercellular adhesion events stabilized by heterophilic Teneurin-4 trans-interactions disrupted latrophilin colocalization with F-actin and led to an isoform-specific rescue of cell extensions. Therefore, we found that constitutive signaling of latrophyllins and their activation by ligand directly involves the actin cytoskeleton machinery

Norma Judith Cruz Ortega

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