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Cell. 2000 Apr 28;101(3):259-70.

Structure of the ERM protein moesin reveals the FERM domain fold masked by an extended actin binding tail domain.

Author information

1
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.

PMID:
10847681
DOI:
10.1016/s0092-8674(00)80836-3
[Indexed for MEDLINE]
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