Abstract
augmented membrane protrusions and cell spreading. Dsg3 colocalizes and forms a complex with ezrin (also phosphorylated form) at the plasma membrane that seemed to be required for proper interaction between ezrin and F-actin since Dsg3 silencing caused significant reduction of the colocalization between ezrin/F-actin or CD44 and collapse of membrane protrusions. Overexpression of Dsg3 elicited an amplified phosphorylation of the threonine residues at the C-terminus of ERM proteins, particularly ezrinThr567. Furthermore, we showed that the enhanced ezrin phosphorylation by Dsg3 could be abrogated substantially by various pharmacological inhibitors including those for PKCs and ROCK that are known to activate ezrin. Conclusion: Our data suggest a novel signaling role for Dsg3 that acts as a transmembrane protein in regulating ezrin activation through various signal molecules including PKCs that are essential in actin-based cell migration, cancer metastasis and progression.
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