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Curr Opin Cell Biol. 1999 Feb;11(1):109-16.

Regulation of cortical structure by the ezrin-radixin-moesin protein family.

Author information

1
Section of Biochemistry, Molecular and Cell Biology Biotechnology Building Cornell University Ithaca NY 14853 USA. apb5@cornell.edu

Abstract

Molecules involved in ERM (ezrin-radixin-moesin) based attachment of membrane proteins to the cortical cytoskeleton in cell surface structures have been identified. In lymphocytes, a direct interaction is seen with extracellular matrix receptors and intercellular adhesion molecules. In polarized epithelial cells, an adaptor molecule named EBP50 provides a bridge between the amino-terminal domain of ezrin and the cytoplasmic regions of plasma membrane proteins, including the cystic fibrosis transmembrane conductance regulator (CFTR) and the beta2 adrenergic receptor. ERM proteins are conformationally regulated - binding sites for EBP50 and F actin are masked in the dormant molecules and activation leads to exposure of these sites. The mechanism of activation, however, remains to be fully elucidated. ERM proteins also play a role in the Rho and Rac signaling pathways: activated ERM proteins can dissociate Rho-GDI (GDP dissociation inhibitor) from Rho and thereby activate Rho-dependent pathways.

PMID:
10047517
DOI:
10.1016/s0955-0674(99)80013-1
[Indexed for MEDLINE]

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