Anillin/Mid1p interacts with the ESCRT-associated protein Vps4p and mitotic kinases to regulate cytokinesis in fission yeast

Imane M Rezig,Wandiahyel G Yaduma,Gwyn W Gould,Christopher J Mcinerny

doi:10.1080/15384101.2021.1962637

Imane M Rezig, Wandiahyel G Yaduma + Show 2 more

Open Access

https://doi.org/10.1080/15384101.2021.1962637

Copy DOI

Journal: Cell Cycle	Publication Date: Aug 14, 2021
Citations: 5	License type: open-access

Affiliation: University of Glasgow, University of Strathclyde

Abstract

ABSTRACT Cytokinesis is the final stage of the cell cycle which separates cellular constituents to produce two daughter cells. Using the fission yeast Schizosaccharomyces pombe we have investigated the role of various classes of proteins involved in this process. Central to these is anillin/Mid1p which forms a ring-like structure at the cell equator that predicts the site of cell separation through septation in fission yeast. Here we demonstrate a direct physical interaction between Mid1p and the endosomal sorting complex required for transport (ESCRT)-associated protein Vps4p, a genetic interaction of the mid1 and vps4 genes essential for cell viability, and a requirement of Vps4p for the correct cellular localization of Mid1p. Furthermore, we show that Mid1p is phosphorylated by aurora kinase, a genetic interaction of the mid1 and the aurora kinase ark1 genes is essential for cell viability, and that Ark1p is also required for the correct cellular localization of Mid1p. We mapped the sites of phosphorylation of Mid1p by human aurora A and the polo kinase Plk1 and assessed their importance in fission yeast by mutational analysis. Such analysis revealed serine residues S332, S523 and S531 to be required for Mid1p function and its interaction with Vps4p, Ark1p and Plo1p. Combined these data suggest a physical interaction between Mid1p and Vps4p important for cytokinesis, and identify phosphorylation of Mid1p by aurora and polo kinases as being significant for this process.

Highlights

Much is understood about the control and reg ulation of the cell division cycle, with many critical cell cycle mechanisms identified being evolutionarily conserved, present across the eukaryotic kingdom
The fission yeast Schizosaccharomyces pombe has proven to be an excellent model organism to study the eukaryotic cell cycle [1]. It is especially useful for studying cytokinesis and cell division as, explicit in its name, it divides by medial fission involving a contractile actomyosin ring leading to the process of cell separation, which is similar to these processes in mammalian cells [2]
We identified and characterized the requirement and role of endosomal sorting complex required for transport (ESCRT) proteins for cyto kinesis in fission yeast [21]. These experiments revealed the interaction of ESCRT proteins with three cell cycle regulators, the Polo-like kinase Plo1p, the aurora kinase Ark1p and the CDC14 phosphatase Clp1p

Summary

Introduction

Much is understood about the control and reg ulation of the cell division cycle, with many critical cell cycle mechanisms identified being evolutionarily conserved, present across the eukaryotic kingdom. The fission yeast Schizosaccharomyces pombe has proven to be an excellent model organism to study the eukaryotic cell cycle [1]. It is especially useful for studying cytokinesis and cell division as, explicit in its name, it divides by medial fission involving a contractile actomyosin ring leading to the process of cell separation, which is similar to these processes in mammalian cells [2]. The SIN proteins form a pathway that facilitates contractile ring constriction and promotes the formation of a medial cell wall-like structure between the two daughter cells, called the septum. A recent study identified anillin/Mid1p as a substrate for Sid2p and indi cated that the phosphorylation of Mid1p facilitates its removal from the cell cortex during the acto myosin contractile ring constriction [7]

Methods

Results

Conclusion