Invertebrate integrins: structure, function, and evolution

Abstract

Integrins are a family of molecules that have fundamental roles in cell-cell and cell-matrix adhesion. It is thought that all metazoan cells have one or more integrin receptors on their surface and that these molecules may have been key in the evolution of multicellularity. Knowledge of the structure, function, and distribution of integrin subunits in invertebrate phyla remains incomplete. However, through the recent use of polymerase chain reaction, integrin subunits have been identified in at least five phyla; sponges, cnidarians, nemadodes, arthropods, and echinoderms. The structure of all of the invertebrate subunits is remarkably similar to that of vertebrate integrin subunits. Some experimental data and patterns of expression indicate that invertebrate integrins have a range of functions similar to those of vertebrate integrins. The ligands are not well characterized but at least two laminin-binding receptors have been identified and two other receptors appear to bind using Arg-Gly-Asp motifs. Invertebrate integrins are present during development, in adults, and on a range of cell types including cells with immunological functions such as hemocytes and coelomocytes. Analysis of the invertebrate beta subunits indicates that the invertebrate integrins have diverged independently within each phylum. The two major clades of vertebrate integrins (beta 1, beta 2, beta 7 and beta 3, beta 5, beta 6, beta 8) appear to have radiated since the divergence of the deuterostomes and there are no distinct orthologous subunits in any of the invertebrate phyla. Since fundamental functions of integrins appear to be conserved, studies of invertebrate integrins have the potential of contributing to our understanding of this important group of receptors.