Ezrin activation by LOK phosphorylation involves a PIP2-dependent wedge mechanism.
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ABSTRACT:
SUBMITTER: Pelaseyed T
PROVIDER: S-EPMC5400502 | biostudies-literature | 2017 Apr
REPOSITORIES: biostudies-literature
Publications
Ezrin activation by LOK phosphorylation involves a PIP<sub>2</sub>-dependent wedge mechanism.
Pelaseyed Thaher T Viswanatha Raghuvir R Sauvanet Cécile C Filter Joshua J JJ Goldberg Michael L ML Bretscher Anthony A
eLife 20170421
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 <i>in vitro</i> system, we now define a multi-step process whereby the kinase LOK specifically phosphorylates ezrin to activate it. Binding of PIP<sub>2</sub> to ezrin induces a conformational change permitting the insertion of ...[more]
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