title: Redundant control of migration and adhesion by ERM proteins in vascular smooth muscle cells.
abstract: Ezrin, radixin, and moesin possess a very similar structure with a C-terminal actin-binding domain and a N-terminal FERM interacting domain. They are known to be involved in cytoskeleton organization in several cell types but their function in vascular smooth muscle cells (VSMC) is still unknown. The aim of this study was to investigate the role of ERM proteins in cell migration induced by PDGF, a growth factor involved in pathophysiological processes like angiogenesis or atherosclerosis. We used primary cultured VSMC obtained from rat aorta, which express the three ERM proteins. Simultaneous depletion of the three ERM proteins with specific siRNAs abolished the effects of PDGF on cell architecture and migration and markedly increased cell adhesion and focal adhesion size, while these parameters were only slightly affected by depletion of ezrin, radixin or moesin alone. Rac1 activation, cell proliferation, and Ca(2+) signal in response to PDGF were unaffected by ERM depletion. These results indicate that ERM proteins exert a redundant control on PDGF-induced VSMC migration by regulating focal adhesion turn-over and cell adhesion to substrate.
authors.affiliation: Laboratory of Cell Physiology, IoNS, Université Catholique de Louvain, Belgium.
authors.forename: Nicolas
authors.initials: N
authors.lastname: Baeyens
authors.forename: Iman
authors.initials: I
authors.lastname: Latrache
authors.forename: Xavier
authors.initials: X
authors.lastname: Yerna
authors.forename: Gauthier
authors.initials: G
authors.lastname: Noppe
authors.forename: Sandrine
authors.initials: S
authors.lastname: Horman
authors.forename: Nicole
authors.initials: N
authors.lastname: Morel
mesh_terms: D000818:Animals; D002448:Cell Adhesion / Q000187:drug effects / Q000502:physiology; D002465:Cell Movement / Q000187:drug effects / Q000502:physiology*; D002478:Cells, Cultured; D003598:Cytoskeletal Proteins / Q000235:genetics / Q000502:physiology*; D022001:Focal Adhesions / Q000187:drug effects / Q000502:physiology*; D008297:Male; D008565:Membrane Proteins / Q000235:genetics / Q000502:physiology*; D008840:Microfilament Proteins / Q000235:genetics / Q000502:physiology*; D009131:Muscle, Smooth, Vascular / Q000166:cytology* / Q000187:drug effects; D032389:Myocytes, Smooth Muscle / Q000187:drug effects / Q000502:physiology*; D010982:Platelet-Derived Growth Factor / Q000494:pharmacology; D011554:Pseudopodia / Q000502:physiology; D051381:Rats; D017208:Rats, Wistar; D000099149:Ezrin
chemical_list: D003598:Cytoskeletal Proteins; D008565:Membrane Proteins; D008840:Microfilament Proteins; D010982:Platelet-Derived Growth Factor; D000099149:Ezrin; C071058:moesin; C071776:radixin
keywords: ERM; Ezrin; Migration; Moesin; PDGF; Radixin; Vascular smooth muscle