Pl-nectin, a discoidin family member, is a ligand for betaC integrins in the sea urchin embryo

Abstract

Pl-nectin is a component of the extracellular matrix that surrounds embryos of the sea urchin Paracentrotus lividus. Pl-nectin mediates adhesion of dissociated embryonic cells to substrates and interfering with ectodermic cells contacting Pl-nectin results in defects in skeleton growth and morphogenesis. Recently, we reported that Pl-nectin is a new member of the discoidin family, in agreement with the notion that many discoidin-containing proteins are involved in cell adhesion processes as integrin ligands. To better understand the molecular basis for the interaction of Pl-nectin with ectoderm, we investigated the hypothesis that Pl-nectin is an integrin ligand in sea urchin embryos. We show that in P. lividus embryos, betaC-containing integrins localize to the apical surface of ectodermic cells, which are in contact with Pl-nectin. Immunoprecipitation experiments indicate that the two proteins are part of a complex in vivo and affinity chromatography indicates that betaC-containing integrin receptors bind purified Pl-nectin. These data support a model in which ectodermic integrins binding to Pl-nectin mediate cellular adhesion to the hyaline layer. Regulated adhesion of cells to the hyaline layer is a critical component of several morphogenetic processes and the identification of the receptors and ligands involved provides new opportunities to investigate the underlying molecular mechanisms of ECM adhesion and morphogenesis.