Coronin is a ubiquitous actin-binding protein representing a member of proteins portraying a WD-repeat sequence, including the β-subunits of trimeric G-proteins. Coronin has been suggested to participate in multiple, actin-based physiological activities such as cell movement and cell division. Although the slow growth of coronin deletion mutants has been attributed to a defect in the fluid-phase uptake of nutrients, the exact role of coronin in cytoskeletal organization has not been elucidated. In this study, we examined a role of coronin in cytokinesis by analyzing the effect of coronin deletion on the actin cytoskeleton and its dynamic distribution using a green fluorescent protein (GFP)-coronin fusion protein. We show that GFP-coronin works similarly to natural coronin in vivo and in vitro. In live cells, GFP- coronin was found to accumulate into the cleavage furrow during cytokinesis. The fluorescence pattern suggests its association to the contractile ring throughout cytokinesis. Interestingly, a substantial amount of coronin was also bound to F-actin at the prospective posterior cortex of the daughter cells. We also show that the coronin null cells reveal irregularities in organization of actin and myosin II and divide by a process identical to the traction-mediated cytofission reported in myosin II mutants. Overall, this study suggests that coronin is essential for organizing the normal actin cytoskeleton and plays a significant role in cell division.
CITATION STYLE
Fukui, Y., Engler, S., Inoué, S., & De Hostos, E. L. (1999). Architectural dynamics and gene replacement of coronin suggest its role in cytokinesis. Cell Motility and the Cytoskeleton, 42(3), 204–217. https://doi.org/10.1002/(SICI)1097-0169(1999)42:3<204::AID-CM4>3.0.CO;2-L
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