Format

Send to

Choose Destination
See comment in PubMed Commons below
Int J Biochem Cell Biol. 2008;40(3):344-9. Epub 2007 Feb 22.

Ezrin/radixin/moesin: versatile controllers of signaling molecules and of the cortical cytoskeleton.

Author information

  • 1Department of Pathology, University of Bern, Murtenstr. 31, CH-3010 Bern, Switzerland. verena.niggli@pathology.unibe.ch

Abstract

Ezrin, radixin and moesin (ERM) proteins are widely distributed proteins located in the cellular cortex, in microvilli and adherens junctions. They feature an N-terminal membrane binding domain linked by an alpha-helical domain to the C-terminal actin-binding domain. In the dormant state, binding sites in the N-terminal domain are masked by interactions with the C-terminal region. The alpha-helical domain also contributes to masking of binding sites. A specific sequence of signaling events results in dissociation of these intramolecular interactions resulting in ERM activation. ERM molecules have been implicated in mediating actin-membrane linkage and in regulating signaling molecules. They are involved in cell membrane organization, cell migration, phagocytosis and apoptosis, and may also play cell-specific roles in tumor progression. Their precise involvement in these processes has yet to be elucidated.

PMID:
17419089
DOI:
10.1016/j.biocel.2007.02.012
[PubMed - indexed for MEDLINE]
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Elsevier Science
    Loading ...
    Support Center