Aurora B Kinase Activity is Required to Prevent Polar Cortical Ingression during Cytokinesis

Miyauchi, Kenji; Zhu, Xiaodong; Foong, Charlene S.F.; Hosoya, Hiroshi; Murata‐Hori, Maki

doi:10.4161/cc.6.20.4817

Cited by 13 publications

(9 citation statements)

References 14 publications

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“…Hesperadin, a small molecule inhibitor of Aurora B, has been used to elucidate the role of Aurora B during cytokinesis (44, 45). Miyauchi et al treated HeLa cells with Hesperadin and observed mis-localization of a number of key cytokinesis proteins, as well as disorganized astral and midzone microtubules.…”

Section: Small Molecule Probes Of Cytokinesismentioning

confidence: 99%

Making the Cut: The Chemical Biology of Cytokinesis

et al. 2010

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Cytokinesis is the last step in the cell cycle, where daughter cells finally separate. Cytokinesis is precisely regulated in both time and space to ensure that each daughter cell receives an equal share of DNA and other cellular materials. Successful completion of cytokinesis, with the cleavage furrow exactly bisecting the axis of chromosome segregation, involves the coordinated action of the cytoskeleton, cell cycle and membrane machineries of cells (1). Chemical biology approaches have been used very successfully to study the mechanism of cytokinesis. In this review, we will discuss the use of small molecule probes to perturb cytokinesis as well as on role that naturally occurring small molecule metabolites such as lipids play during cytokinesis. The mechanism of cytokinesisCytokinesis occurs immediately after mitosis, the division of DNA. The mechanism of cytokinesis has been reviewed in detail elsewhere (1-3). Here, we will briefly introduce key steps to provide context for this review. During mitosis, chromosomes line up in a metaphase plate at the center of the mitotic spindle. As the chromosomes are dividing, a dramatic and poorly understood rearrangement of microtubules takes place and a contractile ring begins to assemble (Figure 1). Contact of the cellular cortex (and plasma membrane?) with microtubule structures is essential for the correct positioning of the contractile ring. Several possible mechanisms have been proposed, although recent studies suggest that multiple mechanisms may occur simultaneously (2,4,5). There are several main signaling pathways, for example those centered around Aurora B and Polo kinases and the small GTPase Rho, that operate and are essential throughout cytokinesis (1). As the location of the cleavage furrow is being specified, the contractile ring begins to assemble. The temporal sequence of protein recruitment to the ring is a significant, but poorly understood mechanistic feature of early cytokinesis. The complete composition of the ring is not known, but the plasma membrane, actin, myosin II and Anillin are clearly important (Figure 1) (6-8). It is not known how the contractile ring is linked to the plasma membrane during ring assembly or ingression. The contractile ring then ingresses, with actin and myosin providing much of the mechanical force (1). We have partial information for the stages of cytokinesis described so far, but the last step, called completion or abscission, remains the least understood. At the end of ingression, a small structure, the midbody, forms. Severing between the daughter cells, which has to be very carefully controlled to avoid the generation of a hole in the cell, occurs in this structure (9). Targeted vesicle transport is thought to play a role both during contractile ring ingression and in generating a membrane barrier that seals the daughter cells during severing (10)(11)(12)(13)(14)(15) (16,17). Insights into the timing of contractile ring assembly during cytokinesis have come from studies in S. pombe (18). Since fungi have many organis...

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Section: Small Molecule Probes Of Cytokinesismentioning

confidence: 99%

Making the Cut: The Chemical Biology of Cytokinesis

et al. 2010

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“…2). Here, it contributes to furrow ingression, central spindle formation, and to axial shortening of chromosomal arms (Douglas et al 2010; Miyauchi et al 2007; Mora-Bermudez et al 2007; Neurohr et al 2011; Petronczki et al 2007; Xu et al 2009). Finally, when present at the midbody, the CPC supports timely abscission (Carlton et al 2012; Norden et al 2006; Steigemann et al 2009).…”

Section: Introductionmentioning

confidence: 99%

Cell division: control of the chromosomal passenger complex in time and space

2013

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The ultimate goal of cell division is equal transmission of the duplicated genome to two new daughter cells. Multiple surveillance systems exist that monitor proper execution of the cell division program and as such ensure stability of our genome. One widely studied protein complex essential for proper chromosome segregation and execution of cytoplasmic division (cytokinesis) is the chromosomal passenger complex (CPC). This highly conserved complex consists of Borealin, Survivin, INCENP, and Aurora B kinase, and has a dynamic localization pattern during mitosis and cytokinesis. Not surprisingly, it also performs various functions during these phases of the cell cycle. In this review, we will give an overview of the latest insights into the regulation of CPC localization and discuss if and how specific localization impacts its diverse functions in the dividing cell.

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“…Cell culture, microscopy and image processing NRK cells and HeLa cells were maintained and grown on glass chamber dishes as previously described (Miyauchi et al, 2007;Mukhina et al, 2007). Live-cell images were acquired and processed as described previously (Mukhina et al, 2007).…”

Section: Methodsmentioning

confidence: 99%

“…For kymographic analysis, time-lapse images of NRK cells expressing CherryFPa-tubulin were acquired using a spinning disk confocal microscopy system (Miyauchi et al, 2007). Regions of interest were then selected and kymograph was generated using Metamorph software (Universal Imaging).…”

Section: Kymographic Analysis and Quantification Of Fluorescence Signalsmentioning

confidence: 99%

Proper positioning of the cleavage furrow requires α-actinin to regulate the specification of different populations of microtubules

Srinivas

Murata‐Hori

2012

Journal of Cell Science

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SummaryProper positioning of the cleavage furrow is essential for successful cell division. The mitotic spindle, which consists of dynamic astral microtubules and stable equatorial microtubules is responsible for this process. However, little is known about how microtubules are regulated in a time-and region-dependent manner. Here, we show that a-actinin-regulated cortical actin filament integrity is crucial to specify different populations of microtubules during cell division in mammalian cells. Depletion of a-actinin caused aberrant recruitment of centralspindlin, but not aurora B or PRC1, to the tips of astral microtubules, leading to a stable association of astral microtubules with the cortex and induction of ectopic furrowing. Depletion of a-actinin also caused impaired assembly of midzone microtubules, leading to a failure of relocation of aurora B to midzone. Our findings unveil an unexpected yet crucial role for an actin crosslinking protein in the regulation of the localization of the microtubule-associated cytokinetic regulator.

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Aurora B Kinase Activity is Required to Prevent Polar Cortical Ingression during Cytokinesis

Cited by 13 publications

References 14 publications

Making the Cut: The Chemical Biology of Cytokinesis

Making the Cut: The Chemical Biology of Cytokinesis

Cell division: control of the chromosomal passenger complex in time and space

Proper positioning of the cleavage furrow requires α-actinin to regulate the specification of different populations of microtubules

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