Key result
Mutations preventing the Cdc12-Cdc15 interaction reduced Cdc12 and F-actin at the contractile ring, delaying its formation during cytokinesis in Schizosaccharomyces pombe.
The F-BAR domain of Cdc15 contributes to contractile ring formation and cytokinesis by directly recruiting the formin Cdc12.
Cdc12 N-terminal motif directs medial targeting; leaves open conservation across species.
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.
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Willet et al. (2015) studied Cytokinesis in Schizosaccharomyces pombe. Mutations preventing Cdc12-Cdc15 interaction vs. Wild-type was evaluated on Contractile ring (CR) formation and cytokinesis. Mutations preventing the Cdc12-Cdc15 interaction reduced Cdc12 and F-actin at the contractile ring, delaying its formation during cytokinesis in Schizosaccharomyces pombe.
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