Conformational Changes in Palladin Actin-Binding Domains Measured by Fluorescent Resonance Energy Transfer

Abstract

The fundamental goal of our research is to understand how cell motility in both normal and metastatic cells is regulated by palladin, an actin binding protein that plays a key role in remodeling the actin cytoskeleton. Our recent work has established that palladin regulates actin dynamics and organization by enhancing the polymerization rate and stabilizing filaments in an orthogonal meshwork. Palladin family members all utilize immunoglobulin-like domains to bind and crosslink actin filaments. Various isoforms of palladin contain from three to five immunoglobulin-like domains that have been implicated in a variety of protein-protein interactions.