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Updated: Feb 15, 2026

Spatiotemporal Analysis of Cytokinetic Events in Fission Yeast
Published on: February 20, 2017
Structure of the fission yeast actomyosin ring during constriction
Matthew T Swulius1,2, Lam T Nguyen1,2, Mark S Ladinsky1
1Division of Biology and Biological Engineering, California Institute of Technology, Pasadena, CA 91125.
Abstract:
Cell division in many eukaryotes is driven by a ring containing actin and myosin. While much is known about the main proteins involved, the precise arrangement of actin filaments within the contractile machinery, and how force is transmitted to the membrane, remains unclear. Here we use cryosectioning and cryofocused ion beam milling to gain access to cryopreserved actomyosin rings in Schizosaccharomyces pombe for direct 3D imaging by electron cryotomography. Our results show that straight, overlapping actin filaments, running nearly parallel to each other and to the membrane, form a loose bundle of ∼150 nm in diameter that "saddles" the inward-bending membrane at the leading edge of the division septum. The filaments do not make direct contact with the membrane. Our analysis of the actin filaments reveals the variability in filament number, nearest-neighbor distances between filaments within the bundle, their distance from the membrane, and angular distribution with respect to the membrane.
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