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Archvillin, a muscle-specific isoform of supervillin, is an early expressed component of the costameric membrane skeleton.
Supervillin binding to myosin II and synergism with anillin are required for cytokinesis.
F-actin and myosin II binding domains in supervillin.
Supervillin reorganizes the actin cytoskeleton and increases invadopodial efficiency.
Novel interactors and a role for supervillin in early cytokinesis.
An N-terminal, 830 residues intrinsically disordered region of the cytoskeleton-regulatory protein supervillin contains Myosin II- and F-actin-binding sites.
Supervillin-mediated suppression of p53 protein enhances cell survival.
Supervillin binds the Rac/Rho-GEF Trio and increases Trio-mediated Rac1 activation.
Supervillin Is a Component of the Hair Cell's Cuticular Plate and the Head Plates of Organ of Corti Supporting Cells.
Unconventional myosins muscle into myofibrils.