A Secreted Protein Promotes Cleavage Furrow Maturation during Cytokinesis

Xu, Xuehong; Vogel, Bruce E.

doi:10.1016/j.cub.2010.12.006

Cited by 67 publications

(83 citation statements)

References 26 publications

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“…A recent study showed that a secreted extracellular matrix protein, hemicentin, regulates cytokinesis (Xu and Vogel, 2011), giving an example of the notion that a secreted ligand and its receptor-mediated signaling is involved in cytokinesis. Therefore, the present data may give another example of the involvement of secreted ligand-activated signaling in cytokinesis.…”

Section: Similar Spatial Localization Of Fz2 and Chmp4b At The Midbodymentioning

confidence: 99%

Wnt5a signaling controls cytokinesis by positioning ESCRT-III to the proper site at the midbody

Fumoto

Kikuchi

Gon

et al. 2012

Journal of Cell Science

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SummaryWnts activate at least two signaling pathways, the b-catenin-dependent and -independent pathways. Although the b-catenin-dependent pathway is known to contribute to G1-S transition, involvement of the b-catenin-independent pathway in cell cycle regulation remains unclear. Here, we show that Wnt5a signaling, which activates the b-catenin-independent pathway, is required for cytokinesis. Dishevelled 2 (Dvl2), a mediator of Wnt signaling pathways, was localized to the midbody during cytokinesis. Beside the localization of Dvl2, Fz2, a Wnt receptor, was detected in the midbody with the endosomal sorting complex required for transport III (ESCRT-III) subunit, CHMP4B. Depletion of Wnt5a, its receptors, and Dvl increased multinucleation. The phenotype observed in Wnt5a-depleted cells was rescued by the addition of purified Wnt5a but not Wnt3a, which is a ligand for the b-catenin-dependent pathway. Moreover, depletion of Wnt5a signaling caused loss of stabilized microtubules and mislocalization of CHMP4B at the midbody, which affected abscission. Inhibition of the stabilization of microtubules at the midbody led to the mislocalization of CHMP4B, while depletion of CHMP4B did not affect the stabilization of microtubules, suggesting that the correct localization of CHMP4B depends on microtubules. Fz2 was localized to the midbody in a Rab11-dependent manner, probably along stabilized microtubules. Fz2 formed a complex with CHMP4B upon Wnt5a stimulation and was required for proper localization of CHMP4B at the midbody, while CHMP4B was not necessary for the localization of Fz2. These results suggest that Wnt5a signaling positions ESCRT-III in the midbody properly for abscission by stabilizing midbody microtubules.

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Section: Similar Spatial Localization Of Fz2 and Chmp4b At The Midbodymentioning

confidence: 99%

Wnt5a signaling controls cytokinesis by positioning ESCRT-III to the proper site at the midbody

Fumoto

Kikuchi

Gon

et al. 2012

Journal of Cell Science

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“…Completion of cytokinesis is coupled to the secretory pathway, which provides new cell membrane and proteins of the extracellular matrix (ECM) (Xu and Vogel, 2011). When cells have defects in secretion of ECM, contractile rings can retract before completion, resulting in multinucleate cells (Xu and Vogel, 2011). Yeast cells assemble an extracellular septum that primarily comprises β-Dglucan and α-D-glucan polymers (Cortes et al, 2012;Humbel et al, 2001) that is essential for the contractile ring constriction (Arasada and Pollard, 2014;Liu et al, 1999;Proctor et al, 2012;Sipiczki and Bozsik, 2000).…”

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

A role for F-BAR protein Rga7p during cytokinesis in S. pombe

Arasada

Pollard

2015

Journal of Cell Science

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F-BAR proteins are known to participate in cytokinesis, but their mechanisms are not well understood. Here we investigated Rga7p an S. pombe F-BAR protein with a RhoGAP domain. Localization of Rga7p to the cytokinetic cleavage furrow depends on its F-BAR domain, actin filaments, formins Cdc12p and For3p, and the presence of a contractile ring. Rga7p is not required for the constriction of the contractile ring but does participate in the transport of a β-glucan synthetase Bgs4p from the late Golgi compartments to the plasma membrane adjacent to the contractile ring. Cells without Rga7p moved Bgs4p normally from the poles to the Golgi apparatus near the cell center, but Bgs4p then moved slowly from the late Golgi compartments to the cleavage site. The late arrival and lower than normal numbers of Bgs4p result in septal defects late in cytokinesis and lysis of separating cells similar to cells with the mutations in the cwg1+ gene encoding Bgs4p.

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“…Although the extracellular matrix is not a rigid structure and does not provide osmotic support, it is considered the functional equivalent of the cell wall, and both structures are essential for the cell (2)(3)(4)(5). In addition, as in fungal cells, some extracellular matrix polymers are also important for cytokinesis (6)(7)(8)(9).…”

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confidence: 99%

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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A Secreted Protein Promotes Cleavage Furrow Maturation during Cytokinesis

Cited by 67 publications

References 26 publications

Wnt5a signaling controls cytokinesis by positioning ESCRT-III to the proper site at the midbody

Wnt5a signaling controls cytokinesis by positioning ESCRT-III to the proper site at the midbody

A role for F-BAR protein Rga7p during cytokinesis in S. pombe

The Cell Biology of Fission Yeast Septation

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