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

J. Cell Biol.. 2015; 
Willet Alaina H,McDonald Nathan A,Bohnert K Adam,Baird Michelle A,Allen John R,Davidson Michael W,Gould Kathle
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Recombinant Antibody Services Submitted: 21 November 2014 Accepted: 9 January 2015 In vitro binding Recombinant proteins conjugated to amylose beads or synthetic biotinylated peptides (5 µg; GenScript) conjugated to streptavidin beads were incubated with recombinant Cdc15 F-BAR for 1 h at 4°C in binding buffer (50 mM Tris-HCl, pH 7. Get A Quote

摘要

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 ... More

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