List of ezrin variants and their localization in OK cells.

<p>Six ezrin constructs were used: <b>A.</b> A full length wild-type ezrin (Ezrin-WT); <b>B.</b> An ezrin in which the binding to PIP2 was abolished by mutation of two double lysines to asparagines, K253/254N and K262/263N, (Ezrin-PIP2^- [<a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0129306#pone.0129306.ref006" target="_blank">6</a>]); <b>C.</b> An ezrin with a threonine to aspartic acid point mutation at position 567 (Ezrin-T/D—phosphothreonine mimic, constitutive active [<a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0129306#pone.0129306.ref041" target="_blank">41</a>]); <b>D.</b> An ezrin with T567D mutation in the PIP2^- ezrin mutant (Ezrin-PIP2^- T/D [<a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0129306#pone.0129306.ref006" target="_blank">6</a>]); <b>E.</b> An ezrin with a threonine to alanine point mutation at position 567 (Ezrin-T/A—non phosphorylable that binds inefficiently to the actin cytoskeleton [<a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0129306#pone.0129306.ref041" target="_blank">41</a>]); <b>F.</b> An ezrin with T567A mutation in the PIP2^- ezrin mutant (Ezrin-PIP2^- T/A [<a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0129306#pone.0129306.ref006" target="_blank">6</a>]). The six ezrin constructs were mEGFP. Localization of ezrin and variants was visualized by indirect immunofluorescence (4 experiments per condition). Highlighted in the figure are XZ cross-sections (plus zoom) and XY face views. Apical localization is indicated by an arrow. Scale bar 2 μm.