The BioGRID | PUBLICATION VIEW

	Cell Apr (2000); 101(3):259-70
Structure of the ERM protein moesin reveals the FERM domain fold masked by an extended actin binding tail domain.
Pearson MA, Reczek D, Bretscher A, Karplus PA
Department of Molecular Biology and Genetics, Cornell University, Ithaca, New York 14853, USA.
Abstract: The ezrin-radixin-moesin (ERM) protein family link actin filaments of cell surface structures to the plasma membrane, using a C-terminal F-actin binding segment and an N-terminal FERM domain, a common membrane binding module. ERM proteins are regulated by an intramolecular association of the FERM and C-terminal tail domains that masks their binding sites. The crystal structure of a dormant moesin FERM/tail complex reveals that the FERM domain has three compact lobes including an integrated PTB/PH/ EVH1 fold, with the C-terminal segment bound as an extended peptide masking a large surface of the FERM domain. This extended binding mode suggests a novel mechanism for how different signals could produce varying levels of activation. Sequence conservation suggests a similar regulation of the tumor suppressor merlin.
[PUBMED: 10847681]