摘要：SummaryCytokinesis is executed by protein networks organized into functional modules. Individual proteins within each module have been characterized to various degrees. However, the collective behavior and interplay of the modules remain poorly understood. In this study, we conducted quantitative time-lapse imaging to analyze the accumulation kinetics of more than 20 proteins from different modules of cytokinesis in budding yeast. This analysis has led to a comprehensive picture of the kinetic landscape of cytokinesis, from actomyosin ring (AMR) assembly to cell separation. It revealed that the AMR undergoes biphasic constriction and that the switch between the constriction phases is likely triggered by AMR maturation and primary septum formation. This analysis also provided further insights into the functions of actin filaments and the transglutaminase-like protein Cyk3 in cytokinesis and, in addition, defined Kre6 as the likely enzyme that catalyzes β-1,6-glucan synthesis to drive cell wall maturation during cell growth and division.Graphical AbstractDisplay OmittedHighlights•Cytokinesis is executed by protein modules each with a unique kinetic signature•Actomyosin ring constricts in a biphasic manner that is elaborately regulated•The transglutaminase-like domain in Cyk3 plays a dual role in cytokinesis•Kre6 catalyzes β-1,6-glucan synthesis at the cell surface during growth and divisionBiological Sciences; Molecular Biology; Cell Biology
