title: Ezrin/radixin/moesin: versatile controllers of signaling molecules and of the cortical cytoskeleton.
abstract: Ezrin, radixin and moesin (ERM) proteins are widely distributed proteins located in the cellular cortex, in microvilli and adherens junctions. They feature an N-terminal membrane binding domain linked by an alpha-helical domain to the C-terminal actin-binding domain. In the dormant state, binding sites in the N-terminal domain are masked by interactions with the C-terminal region. The alpha-helical domain also contributes to masking of binding sites. A specific sequence of signaling events results in dissociation of these intramolecular interactions resulting in ERM activation. ERM molecules have been implicated in mediating actin-membrane linkage and in regulating signaling molecules. They are involved in cell membrane organization, cell migration, phagocytosis and apoptosis, and may also play cell-specific roles in tumor progression. Their precise involvement in these processes has yet to be elucidated.
authors.affiliation: Department of Pathology, University of Bern, Murtenstr. 31, CH-3010 Bern, Switzerland. verena.niggli@pathology.unibe.ch
authors.forename: Verena
authors.initials: V
authors.lastname: Niggli
authors.forename: Jérémie
authors.initials: J
authors.lastname: Rossy
mesh_terms: D000199:Actins / Q000378:metabolism; D022005:Adherens Junctions / Q000502:physiology; D000818:Animals; D003598:Cytoskeletal Proteins / Q000737:chemistry / Q000502:physiology*; D003599:Cytoskeleton / Q000502:physiology*; D006801:Humans; D008565:Membrane Proteins / Q000737:chemistry / Q000502:physiology*; D008840:Microfilament Proteins / Q000737:chemistry / Q000502:physiology*; D008871:Microvilli / Q000502:physiology; D011487:Protein Conformation; D000099149:Ezrin
chemical_list: D000199:Actins; D003598:Cytoskeletal Proteins; D008565:Membrane Proteins; D008840:Microfilament Proteins; D000099149:Ezrin; C071058:moesin; C071776:radixin