A Cdc42 GEF, Gef1, through endocytosis organizes F-BAR Cdc15 along the actomyosin ring and promotes concentric furrowing.
During cytokinesis, fission yeast coordinates actomyosin ring constriction with septum ingression, resulting in concentric furrow formation by a poorly defined mechanism. We report that  Schizosaccharomyces pombe  cells lacking the Cdc42 activator Gef1, combined with an activated allele of the formin, Cdc12, display non-concentric furrowing. Non-concentrically furrowing cells display uneven distribution of the scaffold Cdc15 along the ring. This suggests that, after ring assembly, uniform Cdc15 distribution along the ring enables proper furrow formation. We find that, after assembly, Cdc15 is recruited to the ring in an Arp2/3 complex-dependent manner and is decreased in the activated  cdc12  mutant. Cdc15 at cortical endocytic patches shows increased levels and extended lifetimes in  gef1  and activated  cdc12  mutants. We hypothesize endocytosis helps recruit Cdc15 to assembled rings; uneven Cdc15 distribution at the ring occurs when endocytic patches contain increased Cdc15 levels and the patch-association rate is slow. Based on this, we developed a mathematical model that captures experimentally observed Cdc15 distributions along the ring. We propose that, at the ring, Gef1 and endocytic events promote uniform Cdc15 organization to enable proper septum ingression and concentric furrow formation.
Onwubiko UN, Mlynarczyk PJ, Wei B, Habiyaremye J, Clack A, Abel SM, Das ME