Ezrin, radixin and moesin, collectively known as the ERM proteins, are a group of closely related membrane-cytoskeleton linkers that regulate cell adhesion and cortical morphogenesis. ERM proteins can self-associate through intra- and inter-molecular interactions, and these interactions mask several binding sites on the proteins. ERM activation involves unfolding of the molecule, and allows the protein to bind to plasma membrane components either directly, or indirectly through linker proteins. The discovery that the tumour-suppressor NF2, also known as merlin/schwannomin, is related to ERM proteins has added a new impetus to investigations of their roles. This review discusses current understanding of the structure and function of members of the ERM family of proteins.