Molecular organization of cytokinesis node predicts the constriction rate of the contractile ring

The molecular organization of cytokinesis proteins governs contractile ring function. We used single molecule localization microscopy in live cells to elucidate the molecular organization of cytokinesis proteins and relate it to the constriction rate of the contractile ring. Wild-type fission yeast cells assemble contractile rings by the coalescence of cortical proteins complexes called nodes whereas cells without Anillin/Mid1p (Delta mid1) lack visible nodes yet assemble contractile rings competent for constriction from the looping of strands. We leveraged the Amid1 contractile ring assembly mechanism to determine how two distinct molecular organizations, nodes versus strands, can yield functional contractile rings. Contrary to previous interpretations, nodes assemble in Amid1 cells. Our results suggest that Myo2p heads condense upon interaction with actin filaments and an excess number of Myo2p heads bound to actin filaments hinders constriction thus reducing the constriction rate. Our work establishes a predictive correlation between the molecular organization of nodes and the behavior of the contractile ring.

Automated summary

This study used single molecule localization microscopy in live cells to elucidate the molecular organization of cytokinesis proteins and their impact on the function of the contractile ring. The research revealed that an excess number of Myo2p heads bound to actin filaments hindered constriction, thus reducing the constriction rate. The predictive correlation between the molecular organization of nodes and the behavior of the contractile ring was established.