Regulation of contractile ring formation and septation in Schizosaccharomyces pombe

Willet, Alaina H.; McDonald, Nathan A.; Gould, Kathleen L.

doi:10.1016/j.mib.2015.08.001

Cited by 47 publications

(58 citation statements)

References 59 publications

(68 reference statements)

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“…Thus, when Bgs1 recruitment to the cell middle is delayed by the presence of a compromised Cdc15 function, the AMR slides away from the cell middle (46). As described for Ags1, this delay in Bgs1 recruitment could be explained by a general delay in AMR formation when Cdc15 function is reduced (1,10,89). Despite these observations, it is still unknown whether it is Bgs1 itself or its product that is responsible for the stable AMR maintenance in the cell middle and how this attachment is achieved.…”

Section: Anchorage and Maintenance Of The Amr In The Cell Middle Plasmentioning

confidence: 89%

“…In fission yeast, the nucleus and Mid1 mark the assembly of the AMR in the cell middle (1). However, during and after assembly, this ring must be spatially maintained for a proper cell division.…”

Section: Anchorage and Maintenance Of The Amr In The Cell Middle Plasmentioning

confidence: 99%

“…In animal cells, furrow formation requires the formation, maintenance, and closure of an actomyosin ring (AMR), coupled with the deposition of new plasma membrane material. Fungal cells are surrounded by a rigid cell wall exoskeleton; thus, AMR contraction is tightly coordinated with the biogenesis of a special wall structure named the division septum (1).…”

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confidence: 99%

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The Cell Biology of Fission Yeast Septation

Cortés

Ramos

Osumi

et al. 2016

Microbiol Mol Biol Rev

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SUMMARYIn animal cells, cytokinesis requires the formation of a cleavage furrow that divides the cell into two daughter cells. Furrow formation is achieved by constriction of an actomyosin ring that invaginates the plasma membrane. However, fungal cells contain a rigid extracellular cell wall surrounding the plasma membrane; thus, fungal cytokinesis also requires the formation of a special septum wall structure between the dividing cells. The septum biosynthesis must be strictly coordinated with the deposition of new plasma membrane material and actomyosin ring closure and must occur in such a way that no breach in the cell wall occurs at any time. Because of the high turgor pressure in the fungal cell, even a minor local defect might lead to cell lysis and death. Here we review our knowledge of the septum structure in the fission yeastSchizosaccharomyces pombeand of the recent advances in our understanding of the relationship between septum biosynthesis and actomyosin ring constriction and how the two collaborate to build a cross-walled septum able to support the high turgor pressure of the cell. In addition, we discuss the importance of the septum biosynthesis for the steady ingression of the cleavage furrow.

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Section: Anchorage and Maintenance Of The Amr In The Cell Middle Plasmentioning

confidence: 89%

Section: Anchorage and Maintenance Of The Amr In The Cell Middle Plasmentioning

confidence: 99%

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The Cell Biology of Fission Yeast Septation

Cortés

Ramos

Osumi

et al. 2016

Microbiol Mol Biol Rev

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“…Our understanding of the cytokinetic apparatus is most advanced in fission yeast (16). Only in fission yeast do we know the concentrations of the major cytokinesis proteins (17) and the time course of events leading to cellular division (18,19).…”

mentioning

confidence: 99%

Molecular organization of cytokinesis nodes and contractile rings by super-resolution fluorescence microscopy of live fission yeast

Laplante

Huang

Tebbs

et al. 2016

Proc. Natl. Acad. Sci. U.S.A.

122

280

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Cytokinesis in animals, fungi, and amoebas depends on the constriction of a contractile ring built from a common set of conserved proteins. Many fundamental questions remain about how these proteins organize to generate the necessary tension for cytokinesis. Using quantitative high-speed fluorescence photoactivation localization microscopy (FPALM), we probed this question in live fission yeast cells at unprecedented resolution. We show that nodes, protein assembly precursors to the contractile ring, are discrete structural units with stoichiometric ratios and distinct distributions of constituent proteins. Anillin Mid1p, Fes/CIP4 homology-Bin/amphiphysin/ Rvs (F-BAR) Cdc15p, IQ motif containing GTPase-activating protein (IQGAP) Rng2p, and formin Cdc12p form the base of the node that anchors the ends of myosin II tails to the plasma membrane, with myosin II heads extending into the cytoplasm. This general node organization persists in the contractile ring where nodes move bidirectionally during constriction. We observed the dynamics of the actin network during cytokinesis, starting with the extension of short actin strands from nodes, which sometimes connected neighboring nodes. Later in cytokinesis, a broad network of thick bundles coalesced into a tight ring around the equator of the cell. The actin ring was ∼125 nm wide and ∼125 nm thick. These observations establish the organization of the proteins in the functional units of a cytokinetic contractile ring.T he mechanism of cell division by a contractile ring of actin and myosin II appeared in the common ancestor of amoebas, fungi, and animals (1). Although much is known about the protein composition of contractile rings, relatively little is known about the 3D organization of these proteins. This information is required to formulate computer models and simulations to test ideas regarding the mechanisms of contractile ring function.Electron microscopy has shown actin filaments in contractile rings of animal cells (2, 3) and yeast cells (4,5). Myosin II concentrates in cleavage furrow (6) and is the main motor for constricting contractile rings (7,8). In animal cells, electron microscopy has revealed rods the size of myosin II minifilaments in contractile rings (2, 9), and structured-illumination fluorescence microscopy has shown that this myosin II is organized in bipolar assemblies (10). Contractile rings contain other structural and regulatory proteins, including anillin (11), IQ motif containing GTPase-activating proteins (IQGAP) (12), formins (13), alphaactinin (14), and Fes/CIP4 homology-Bin/amphiphysin/Rvs (F-BAR) proteins (15), but how these proteins are anchored to the plasma membrane or organized into functional complexes in animal cells is unknown.Our understanding of the cytokinetic apparatus is most advanced in fission yeast (16). Only in fission yeast do we know the concentrations of the major cytokinesis proteins (17) and the time course of events leading to cellular division (18,19). Molecularly explicit computer models can account for both the ...

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“…cell division | Streptococcus pneumoniae | SMC | chromosome organization | FtsZ I n eukaryotic cells, DNA replication, chromosome segregation, and cell division are tightly coordinated and separated in time (1)(2)(3). In most bacteria, this is less obvious as these processes occur simultaneously.…”

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confidence: 99%

Chromosome segregation drives division site selection in Streptococcus pneumoniae

Raaphorst

Kjos

Veening

2017

Proc. Natl. Acad. Sci. U.S.A.

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Accurate spatial and temporal positioning of the tubulin-like protein FtsZ is key for proper bacterial cell division. Streptococcus pneumoniae (pneumococcus) is an oval-shaped, symmetrically dividing opportunistic human pathogen lacking the canonical systems for division site control (nucleoid occlusion and the Min-system). Recently, the early division protein MapZ was identified and implicated in pneumococcal division site selection. We show that MapZ is important for proper division plane selection; thus, the question remains as to what drives pneumococcal division site selection. By mapping the cell cycle in detail, we show that directly after replication both chromosomal origin regions localize to the future cell division sites, before FtsZ. Interestingly, Z-ring formation occurs coincidently with initiation of DNA replication. Perturbing the longitudinal chromosomal organization by mutating the condensin SMC, by CRISPR/Cas9-mediated chromosome cutting, or by poisoning DNA decatenation resulted in mistiming of MapZ and FtsZ positioning and subsequent cell elongation. Together, we demonstrate an intimate relationship between DNA replication, chromosome segregation, and division site selection in the pneumococcus, providing a simple way to ensure equally sized daughter cells.

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Regulation of contractile ring formation and septation in Schizosaccharomyces pombe

Cited by 47 publications

References 59 publications

The Cell Biology of Fission Yeast Septation

The Cell Biology of Fission Yeast Septation

Molecular organization of cytokinesis nodes and contractile rings by super-resolution fluorescence microscopy of live fission yeast

Chromosome segregation drives division site selection in Streptococcus pneumoniae

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