ERM proteins in cell adhesion and membrane dynamics

Ezrin, radixin and moesin, collectively known as the ERM proteins, are a group of closely related membrane–cytoskeleton linkers that regulate cell adhesion and cortical morphogenesis. ERM proteins can self-associate through intra- and inter-molecular interactions, and these interactions mask several...

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Bibliographic Details
Published in:Trends in Cell Biology 1999-05, Vol.9 (5), p.187-192
Main Authors: Mangeat, Paul, Roy, Christian, Martin, Marianne
Format: Article
Language:English
Subjects:
Blood Proteins - physiology
cell adhesion
Cell Adhesion - physiology
Cell Membrane - chemistry
Cell Membrane - physiology
Cytoskeletal Proteins
cytoskeleton
ERM protein
Ezrin
Humans
Membrane Proteins - physiology
merlin
merlin protein
Microfilament Proteins - physiology
moesin
neurofibromatosis
NF2 protein
Phosphoproteins - physiology
radixin
schwannomin
Tumor Cells, Cultured - chemistry
Tumor Cells, Cultured - cytology
Tumor Cells, Cultured - physiology
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Summary:Ezrin, radixin and moesin, collectively known as the ERM proteins, are a group of closely related membrane–cytoskeleton linkers that regulate cell adhesion and cortical morphogenesis. ERM proteins can self-associate through intra- and inter-molecular interactions, and these interactions mask several binding sites on the proteins. ERM activation involves unfolding of the molecule, and allows the protein to bind to plasma membrane components either directly, or indirectly through linker proteins. The discovery that the tumour-suppressor NF2, also known as merlin/schwannomin, is related to ERM proteins has added a new impetus to investigations of their roles. This review discusses current understanding of the structure and function of members of the ERM family of proteins.
ISSN:0962-8924
1879-3088
DOI:10.1016/S0962-8924(99)01544-5