The actomyosin network is influenced by NMHC IIA and regulated by Crp^F46, which is involved in controlling cell migration.

When a cell migrates, the centrosome positions between the nucleus and the leading edge of migration via the microtubule system. The protein Crp^F46 (centrosome-related protein F46) has a known role during mitosis and centrosome duplication. However, how Crp^F46 efficiently regulates centrosome-related cell migration is unclear. Here, we report that knockdown of Crp^F46 resulted in the disruption of microtubule arrangement, with impaired centrosomal reorientation, and slowed down cell migration. In cells that express low levels of Crp^F46, stress fibers were weakened, which could be rescued by recovering Flag-Crp^F46. We also found that Crp^F46 interacted with non-muscle myosin high chain IIA (NMHC IIA) and that its three coiled-coil domains are pivotal for its binding to NMHC IIA. Additionally, analyses of phosphorylation of NMHC IIA and RLC (regulatory light chain) demonstrated that Crp^F46 was associated with myosin IIA during filament formation. Indirect immunofluorescence images indicated that NM IIA filaments were inhibited when Crp^F46 was under-expressed. Thus, Crp^F46 regulates cell migration by centrosomal reorientation and altering the function of the actomyosin network by controlling specific phosphorylation of myosin.

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