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The F-BAR Cdc15 promotes contractile ring formation through the direct recruitment of the formin Cdc12.

AUTHORS

Willet AHAlaina H , McDonald NA Nathan A , Bohnert KA K Adam , Baird MA Michelle A , Allen JR John R , Davidson MW Michael W , Gould KL Kathleen L . The Journal of cell biology. 2015 2 16; 208(4). 391-9

ABSTRACT

In Schizosaccharomyces pombe, cytokinesis requires the assembly and constriction of an actomyosin-based contractile ring (CR). Nucleation of F-actin for the CR requires a single formin, Cdc12, that localizes to the cell middle at mitotic onset. Although genetic requirements for formin Cdc12 recruitment have been determined, the molecular mechanisms dictating its targeting to the medial cortex during cytokinesis are unknown. In this paper, we define a short motif within the N terminus of Cdc12 that binds directly to the F-BAR domain of the scaffolding protein Cdc15. Mutations preventing the Cdc12-Cdc15 interaction resulted in reduced Cdc12, F-actin, and actin-binding proteins at the CR, which in turn led to a delay in CR formation and sensitivity to other perturbations of CR assembly. We conclude that Cdc15 contributes to CR formation and cytokinesis via formin Cdc12 recruitment, defining a novel cytokinetic function for an F-BAR domain.