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.
Publication types
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Research Support, U.S. Gov't, Non-P.H.S.
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Actins / metabolism*
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Amino Acid Sequence
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Binding Sites
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Crystallography, X-Ray
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Cytoskeletal Proteins*
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Humans
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Membrane Proteins / chemistry
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Microfilament Proteins / chemistry*
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Microfilament Proteins / genetics
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Microfilament Proteins / metabolism
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Models, Molecular
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Molecular Sequence Data
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Neurofibromin 2
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Neuropeptides*
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Protein Folding*
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Protein Structure, Tertiary
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Recombinant Fusion Proteins / chemistry
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Recombinant Fusion Proteins / genetics
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Recombinant Fusion Proteins / metabolism
Substances
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Actins
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Cytoskeletal Proteins
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Membrane Proteins
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Microfilament Proteins
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Neurofibromin 2
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Neuropeptides
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Recombinant Fusion Proteins
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erythrocyte membrane band 4.1 protein
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erythrocyte membrane protein band 4.1-like 1
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moesin