Journal
CELL
Volume 101, Issue 3, Pages 259-270Publisher
CELL PRESS
DOI: 10.1016/S0092-8674(00)80836-3
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Funding
- NCRR NIH HHS [RR-01646] Funding Source: Medline
- NIGMS NIH HHS [GM08500, GM36652] Funding Source: Medline
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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.
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