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Ezrin activation by LOK phosphorylation involves a PIP2-dependent wedge mechanism.

Journal article
Authors Thaher Pelaseyed
Raghuvir Viswanatha
Cécile Sauvanet
Joshua J Filter
Michael L Goldberg
Anthony Bretscher
Published in eLife
Volume 6
ISSN 2050-084X
Publication year 2017
Published at
Language en
Links dx.doi.org/10.7554/eLife.22759
www.ncbi.nlm.nih.gov/entrez/query.f...
Subject categories Cell Biology, Biochemistry

Abstract

How cells specify morphologically distinct plasma membrane domains is poorly understood. Prior work has shown that restriction of microvilli to the apical aspect of epithelial cells requires the localized activation of the membrane-F-actin linking protein ezrin. Using an in vitro system, we now define a multi-step process whereby the kinase LOK specifically phosphorylates ezrin to activate it. Binding of PIP2 to ezrin induces a conformational change permitting the insertion of the LOK C-terminal domain to wedge apart the membrane and F-actin-binding domains of ezrin. The N-terminal LOK kinase domain can then access a site 40 residues distal from the consensus sequence that collectively direct phosphorylation of the appropriate threonine residue. We suggest that this elaborate mechanism ensures that ezrin is only phosphorylated at the plasma membrane, and with high specificity by the apically localized kinase LOK.

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