Comparative Analysis of the Roles of Non-muscle Myosin-IIs in Cytokinesis in Budding Yeast, Fission Yeast, and Mammalian Cells.

Kangji Wang,Hiroki Okada,Erfei Bi

doi:10.3389/fcell.2020.593400

Kangji Wang, Hiroki Okada + Show 1 more

Open Access

https://doi.org/10.3389/fcell.2020.593400

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Abstract

The contractile ring, which plays critical roles in cytokinesis in fungal and animal cells, has fascinated biologists for decades. However, the basic question of how the non-muscle myosin-II and actin filaments are assembled into a ring structure to drive cytokinesis remains poorly understood. It is even more mysterious why and how the budding yeast Saccharomyces cerevisiae, the fission yeast Schizosaccharomyces pombe, and humans construct the ring structure with one, two, and three myosin-II isoforms, respectively. Here, we provide a comparative analysis of the roles of the non-muscle myosin-IIs in cytokinesis in these three model systems, with the goal of defining the common and unique features and highlighting the major questions regarding this family of proteins.

Highlights

Non-muscle myosin-IIs (NM-IIs) play critical roles in many fundamental processes including cytokinesis, cell adhesion, cell migration, exocytosis, and tissue morphogenesis (VicenteManzanares et al, 2009; Shutova and Svitkina, 2018)
Several important lessons are learned through the comparative analysis of the roles of the NM-II isoforms in cytokinesis in budding yeast, fission yeast, and mammalian cells
The NM-IIs in all three systems assemble into a functional actomyosin ring (AMR) in anaphase and constrict to drive furrow ingression

Summary

Introduction

Non-muscle myosin-IIs (NM-IIs) play critical roles in many fundamental processes including cytokinesis, cell adhesion, cell migration, exocytosis, and tissue morphogenesis (VicenteManzanares et al, 2009; Shutova and Svitkina, 2018). The NM-II heavy chains Myh9, Myh10, and Myh14 in mammalian cells share a similar domain organization as the myosin-II heavy chains in budding yeast and fission yeast, a globular head domain with actin-binding and ATPase activities, IQ1 and IQ2 motifs where an ELC and an RLC bind, respectively, and a rod-shaped tail that is made of CCs, followed by a small NHR in each isoform (Figure 1).

Results

Conclusion