Novel WRC interacting receptors transducing signals at the membrane to the actin cytoskeleton

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Cell shape changes require a dynamic interplay between membrane remodeling and the actin cytoskeleton by which environmental signals are translated into changes in morphol-ogy and motility. The WASP family verprolin homologous (WAVE) protein is a key activator of the Arp2/3 complex and coordinates actin nucleation in many cellular processes including adhesion, migration and phagocytosis. The WAVE protein is constitutively incor-porated into a conserved, heteropentameric complex, the WAVE regulatory complex (WRC) that controls its activity in time and space. We recently described a novel mecha-nism by which the WRC can directly be recruited to membranes through a conserved pep-tide motif (WIRS) found in a variety of transmembrane and membrane-associated proteins. This provides a new signaling platform by which environmental signals might be translated into changes in morphology and motility. Here, we will analyze collective follicle cell migration in Drosophila oogenesis and wound-induced directed single cell migration of Drosophila immune cells and dissect how these WIRS surface receptors bridge ligands to changes of the actin cytoskeleton.