Cytokinesis In Animal Cells Research Articles

Microtuble organization in Xenopus eggs during the first cleavage and its role in cytokinesis.

It has been suggested that the organization of microtubules during mitosis plays an important role in cytokinesis in animal cells. We studied the organization of microtubules during the first cleavage and its role in cytokinesis of Xenopus eggs. First, we examined the immunofluorescent localization of microtubules in Xenopus eggs at various stages during the first cleavage. The astral microtubules that extend from each of the two centrosomes towards the division plane meet and connect with each other at the division plane as cytokinesis proceeds. The microtubular connection thus advances from the animal pole to the vegetal pole, and its leading edge is located approximately beneath the leading edge of the cleavage furrow. Furthermore, an experiment using nocodazole suggests that microtubules have an essential role in advancement of the cleavage furrow, but neither in contraction nor maintenance of the already formed contractile ring which underlies the cleavage furrow membrane. These results suggest that the astral microtubules play an important role in controlling the formation of the contractile ring in Xenopus eggs.

Taking tea with actin and microtubules

Microtubule plus ends may control sites of cell polarity and cytokinesis in both animal and yeast cells, but the mechanisms behind this have remained obscure. Now Fred Chang and colleagues at Columbia University, New York, NY, have detected a protein complex in Schizosaccharomyces pombe that links the actin- and microtubule-based cytoskeletal systems. Its existence also suggests that microtubule plus ends polarize cells by targeting cell-polarity factors to the cell surface. Figure Polarity failure in fission yeast results in T-shaped cells. The two proteins that coimmunoprecipitate are the microtubule-associated Tea1 protein and the actin-associated Bud6 protein. Tea1p is constantly deposited at cell tips by the plus ends of microtubules. The cell end that has grown before does not need Tea1p to continue growing, but delivery of Tea1p to the new end is apparently necessary for both the initiation of new growth and, according to Chang, the maintenance of Bud6p at this site. The two proteins are found in large multiprotein complexes that may drive the formation of actin-based structures necessary for growth. ▪

Centrosome-dependent exit of cytokinesis in animal cells.

As an organelle coupling nuclear and cytoplasmic divisions, the centrosome is essential to mitotic fidelity, and its inheritance could be critical to understanding cell transformation. Investigating the behavior of the centrosome in living mitotic cells, we documented a transient and remarkable postanaphase repositioning of this organelle, which apparently controls the release of central microtubules from the midbody and the completion of cell division. We also observed that the absence of the centrosome leads to defects in cytokinesis. Together with recent results in yeasts, our data point to a conserved centrosome-dependent pathway that integrates spatial controls into the decision of completing cell division, which requires the repositioning of the centrosome organelle.

Drosophila male meiosis as a model system for the study of cytokinesis in animal cells.

Drosophila male meiosis offers unique opportunities for mutational dissection of cytokinesis. This system allows easy and unambiguos identification of mutants defective in cytokinesis through the examination of spermatid morphology. Moreover, cytokinesis defects and protein immunostaining can be analyzed with exquisite cytological resolution because of the large size of meiotic spindles. In the past few years several mutations have been isolated that disrupt meiotic cytokinesis in Drosophila males. These mutations specify genes required for the assembly, proper constriction or disassembly of the contractile ring. Molecular characterization of these genes has identified essential components of the cytokinetic machinery, highlighting the role of the central spindle during cytokinesis. This structure appears to be both necessary and sufficient for signaling cytokinesis. In addition, many data indicate that the central spindle microtubules cooperatively interact with elements of the actomyosin contractile ring, so that impairment of either of these structures prevents the formation of the other.

Lava lamp, a novel peripheral golgi protein, is required for Drosophila melanogaster cellularization.

Drosophila cellularization and animal cell cytokinesis rely on the coordinated functions of the microfilament and microtubule cytoskeletal systems. To identify new proteins involved in cellularization and cytokinesis, we have conducted a biochemical screen for microfilament/microtubule-associated proteins (MMAPs). 17 MMAPs were identified; seven have been previously implicated in cellularization and/or cytokinesis, including KLP3A, Anillin, Septins, and Dynamin. We now show that a novel MMAP, Lava Lamp (Lva), is also required for cellularization. Lva is a coiled-coil protein and, unlike other proteins previously implicated in cellularization or cytokinesis, it is Golgi associated. Our functional analysis shows that cellularization is dramatically inhibited upon injecting anti-Lva antibodies (IgG and Fab) into embryos. In addition, we show that brefeldin A, a potent inhibitor of membrane trafficking, also inhibits cellularization. Biochemical analysis demonstrates that Lva physically interacts with the MMAPs Spectrin and CLIP190. We suggest that Lva and Spectrin may form a Golgi-based scaffold that mediates the interaction of Golgi bodies with microtubules and facilitates Golgi-derived membrane secretion required for the formation of furrows during cellularization. Our results are consistent with the idea that animal cell cytokinesis depends on both actomyosin-based contraction and Golgi-derived membrane secretion.

CYK-4: A Rho family gtpase activating protein (GAP) required for central spindle formation and cytokinesis.

During cytokinesis of animal cells, the mitotic spindle plays at least two roles. Initially, the spindle positions the contractile ring. Subsequently, the central spindle, which is composed of microtubule bundles that form during anaphase, promotes a late step in cytokinesis. How the central spindle assembles and functions in cytokinesis is poorly understood. The cyk-4 gene has been identified by genetic analysis in Caenorhabditis elegans. Embryos from cyk-4(t1689ts) mutant hermaphrodites initiate, but fail to complete, cytokinesis. These embryos also fail to assemble the central spindle. We show that the cyk-4 gene encodes a GTPase activating protein (GAP) for Rho family GTPases. CYK-4 activates GTP hydrolysis by RhoA, Rac1, and Cdc42 in vitro. RNA-mediated interference of RhoA, Rac1, and Cdc42 indicates that only RhoA is essential for cytokinesis and, thus, RhoA is the likely target of CYK-4 GAP activity for cytokinesis. CYK-4 and a CYK-4:GFP fusion protein localize to the central spindle and persist at cell division remnants. CYK-4 localization is dependent on the kinesin-like protein ZEN-4/CeMKLP1 and vice versa. These data suggest that CYK-4 and ZEN-4/CeMKLP1 cooperate in central spindle assembly. Central spindle localization of CYK-4 could accelerate GTP hydrolysis by RhoA, thereby allowing contractile ring disassembly and completion of cytokinesis.

A myosin light chain mediates the localization of the budding yeast IQGAP-like protein during contractile ring formation.

Cytokinesis in animal cells is accomplished through constriction of an actomyosin ring [1] [2] [3], which must assemble at the correct time and place in order to ensure proper division of genetic material and organelles. Budding yeast is a useful model system for determining the biochemical pathway of contractile ring assembly. The budding yeast IQGAP-like protein, Cyk1/Iqg1p, has multiple roles in the assembly and contraction of the actomyosin ring [4] [5] [6]. Previously, the IQ motifs of Cyk1/Iqg1p were shown to be required for the localization of this protein at the bud neck [6]. We have investigated the binding partner of the IQ motifs, which are predicted to interact with calmodulin-like proteins. Mlc1p was originally identified as a light chain for a type V myosin, Myo2p; however, a cytokinesis defect associated with disruption of the MLC1 gene suggested that the essential function of Mlc1p may involve interactions with other proteins [7]. We show that Mlc1p binds the IQ motifs of Cyk1/Iqg1p and present evidence that this interaction recruits Cyk1/Iqg1p to the bud neck. Immunofluorescence staining shows that Mlc1p is localized to sites of polarized cell growth as well as the bud neck before and independently of Cyk1p. These results demonstrate that Mlc1p is important for the assembly of the actomyosin ring in budding yeast and that this function is mediated through interaction with Cyk1/Iqg1p.

Relationships between the central spindle and the contractile ring during cytokinesis in animal cells

Relationships between the central spindle and the contractile ring during cytokinesis in animal cells

Relationships between the central spindle and the contractile ring during cytokinesis in animal cells

Relationships between the central spindle and the contractile ring during cytokinesis in animal cells

Relationships between the central spindle and the contractile ring during cytokinesis in animal cells

During late anaphase and telophase, animal cells develop a bundle of antiparallel, interdigitating microtubules between the two daughter nuclei. Recent data indicate that this structure, called the central spindle, plays an essential role during cytokinesis. Studies in Drosophila and on vertebrate cells strongly suggest that the molecular signals for cytokinesis specifically emanate from the central spindle midzone. Moreover, the analysis of Drosophila mutants defective in cytokinesis has revealed a cooperative interaction between the central spindle microtubules and the contractile ring: when either of these structures is perturbed, the proper assembly of the other is disrupted. Based on these results we propose a model for the role of the central spindle during cytokinesis. We suggest that the interaction between central spindle microtubules and cortical actin filaments leads to two early events crucial for cytokinesis: the positioning of the contractile ring, and the stabilization of the plus ends of the interdigitating microtubules that comprise the central spindle. The latter event would provide the cell with a specialized microtubule scaffold that could mediate the translocation of plus-end-directed molecular motors to the cell's equator. Among the cargoes transported by these motors could be proteins involved in the regulation and execution of cytokinesis.

Cell division: Plant-like properties of animal cell cytokinesis

Recent evidence that a syntaxin is required for cytokinesis in Caenorhabditis elegans embryos suggests that the mechanism of cell division in plant and animal cells may be more similar than previously imagined.

Role of myosin II tail sequences in its function and localization at the cleavage furrow in Dictyostelium.

Cytoplasmic myosin II accumulates in the cleavage furrow and provides the force for cytokinesis in animal and amoeboid cells. One model proposes that a specific domain in the myosin II tail is responsible for its localization, possibly by interacting with a factor concentrated in the equatorial region. To test this possibility, we have expressed myosins carrying mutations in the tail domain in a strain of Dictyostelium cells from which the endogenous myosin heavy chain gene has been deleted. The mutations used in this study include four internal tail deletions: Mydelta824-941, Mydelta943-1464, Mydelta943-1194 and Mydelta1156-1464. Contrary to the prediction of the hypothesis, immunofluorescence staining demonstrated that all mutant myosins were able to move toward the furrow region. Chimeric myosins, which consisted of a Dictyostelium myosin head and chicken skeletal myosin tail, also efficiently localized to the cleavage furrow. All these deletion and chimeric mutant myosins, except for Mydelta943-1464, the largest deletion mutant, were able to support cytokinesis in suspension. Our data suggest that there is no single specific domain in the tail of Dictyostelium myosin II that is required for its functioning at and localization to the cleavage furrow.

Regulation of cytokinesis.

At the end of mitosis, daughter cells are separated from each other by cytokinesis. This process involves equal partitioning and segregation of cytoplasm between the two cells. Despite years of study, the mechanism driving cytokinesis in animal cells is not fully understood. Actin and myosin are major components of the contractile ring, the structure at the equator between the dividing cells that provides the force necessary to constrict the cytoplasm. Despite this, there are also tantalizing results suggesting that cytokinesis can occur in the absence of myosin. It is unclear what the roles are of the few other contractile ring components identified to date. While it has been difficult to identify important proteins involved in cytokinesis, it has been even more challenging to pinpoint the regulatory mechanisms that govern this vital process. Cytokinesis must be precisely controlled both spatially and temporally; potential regulators of these parameters are just beginning to be identified. This review discusses the recent progress in our understanding of cytokinesis in animal cells and the mechanisms that may regulate it.

Cytokinesis in Animal Cells.R. Rappaport

Previous articleNext article No AccessNew Biological BooksCytokinesis in Animal Cells. R. Rappaport Richard H. Colby and Rosalind L. HerlandsRichard H. Colby Search for more articles by this author and Rosalind L. Herlands Search for more articles by this author PDFPDF PLUS Add to favoritesDownload CitationTrack CitationsPermissionsReprints Share onFacebookTwitterLinkedInRedditEmail SectionsMoreDetailsFiguresReferencesCited by The Quarterly Review of Biology Volume 73, Number 3Sep., 1998 Published in association with Stony Brook University Article DOIhttps://doi.org/10.1086/420331 Copyright 1998 The University of ChicagoPDF download Crossref reports no articles citing this article.

Cytokinesis in animal cells

Cytokinesis in animal cells

Cytokinesis in fission yeast Schizosaccharomyces pombe

Publisher Summary This chapter discusses the cytokinesis in fission yeast Schizosaccharomyces pombe. The process of cytokinesis in animal cells has been the subject of a large number of ingenious embryological experiments. While these experiments have revealed a great deal at a mechanistic level about what factors influence cleavage furrow formation, much less is known at a molecular level. Because much of the current understanding of the eukaryotic cell cycle at a molecular level is derived from genetic studies in the two yeasts, Saccharomyces cerevisiae and Schizosaccharomyces pombe, it seems likely that the study of cytokinesis in yeast will also be revealing. Schizosaccharomyces pombe is particularly well suited for the study of cytokinesis, because like higher eukaryotes, S. pombe divides by medial fission through the use of an F-actin contractile ring. The actin cytoskeleton in fission yeast contains three major types of actin structures.

Relationship of actin, microtubules, and crosswall synthesis during septation in Aspergillus nidulans.

Studies of cytokinesis in animal cells demonstrate that microtubules play an important role in signaling the position of the actin-containing contractile ring and subsequent formation of the cleavage furrow. Septation in several fungi closely resembles animal cell cytokinesis in that a circumferential ring of actin is visible at the incipient division site. However, this does not necessarily mean that division is contractile since actin may also serve to localize septal wall synthesis. In addition, several studies in fission yeast have suggested that microtubules are dispensable for actin ring formation. We have used synchronized cells and fluorescence microscopy to follow actin structures, nuclear division and septal wall synthesis during septation in Aspergillus nidulans. Our data suggest that actin first appears at the septum site as a circumferential ring and that it later broadens and invaginates, forming an hourglass-shaped structure coincident with septal cell wall synthesis. Depolymerization of microtubules early in septation prevents circumferential actin ring formation. Depolymerization of microtubules after circumferential actin ring formation blocks both the progression to invaginating bands and septal wall synthesis. In contrast to studies in yeast cells, our data suggest that microtubules are required for both the initiation and progression of septation in A. nidulans.

Cell Division: Septins in common?

Two apparently quite distinct processes, cytokinesis in animal cells and in budding yeast cells, have been shown to involve proteins of the same family, the septins, suggesting that the two may not be so different after all.

A fluid mechanical model of cytokinesis in animal cells

A fluid mechanical model of cytokinesis in animal cells

Role of Microtubules in Stimulating Cytokinesis in Animal Cellsa

The initiation of furrow formation is disrupted when microtubule elongation to the cell surface is inhibited either by promoting microtubule disassembly with hydrostatic pressure or by stabilizing the mitotic astral microtubules with taxol. The pressure studies confirmed Rappaport's earlier observation that stimulation of furrow formation is produced by a pair of asters and does not require chromosomes or a central spindle in the large dividing cells of echinoderm embryos. The taxol studies showed that furrow formation occurs between two stable asters when the asters are within 20 microns of the lateral cell surface. Furrow formation at the lateral edge of the cell does not appear to require microtubule dynamics, microtubule elongation, or contact of microtubule ends with the lateral cell surface. Microtubules may function to increase the concentrations of the active forms of diffusible stimulatory factors that interact with receptors at the inner cell surface to initiate the formation of the furrow apparatus and activate contraction.