Cytokinesis D is Mediated by Cortical Flow of Dividing Cells Instead of Chemotaxis

Tanaka, Yuki; Jahan, Md. Golam Sarowar; Kondo, Tomo; Nakano, Masaki; Yumura, Shigehiko

doi:10.3390/cells8050473

Cited by 11 publications

(10 citation statements)

References 22 publications

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“…This is in contrast to the non-parasitic amoeba Dictyostelium , which does form a myosin-based contractile ring (De Lozanne and Spudich, 1987; Fukui, 1990; Fukui and Inoue, 1991), although since Dictyostelium cells lack a midbody, they utilize traction or external forces to complete abscission (Taira and Yumura, 2017). The Entamoeba intercellular bridge is severed mechanically as cells pull apart, although ~30% of cell cleavage events are aided by a helper or “midwife” cell migrating through the bridge, providing external mechanical force to ensure its scission (Biron et al, 2001; Mukherjee et al, 2009; Krishnan and Ghosh, 2018) (Figures 3A,B), as also observed in Dictyostelium (Tanaka et al, 2019). 10–20% of initiated cytokinetic events in Entamoeba are unsuccessful; the intercellular bridge retracts and daughter cells re-fuse.…”

Section: Cytokinesis In the Amoebozoamentioning

confidence: 91%

Who Needs a Contractile Actomyosin Ring? The Plethora of Alternative Ways to Divide a Protozoan Parasite

Hammarton

2019

Front. Cell. Infect. Microbiol.

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Cytokinesis, or the division of the cytoplasm, following the end of mitosis or meiosis, is accomplished in animal cells, fungi, and amoebae, by the constriction of an actomyosin contractile ring, comprising filamentous actin, myosin II, and associated proteins. However, despite this being the best-studied mode of cytokinesis, it is restricted to the Opisthokonta and Amoebozoa, since members of other evolutionary supergroups lack myosin II and must, therefore, employ different mechanisms. In particular, parasitic protozoa, many of which cause significant morbidity and mortality in humans and animals as well as considerable economic losses, employ a wide diversity of mechanisms to divide, few, if any, of which involve myosin II. In some cases, cell division is not only myosin II-independent, but actin-independent too. Mechanisms employed range from primitive mechanical cell rupture (cytofission), to motility- and/or microtubule remodeling-dependent mechanisms, to budding involving the constriction of divergent contractile rings, to hijacking host cell division machinery, with some species able to utilize multiple mechanisms. Here, I review current knowledge of cytokinesis mechanisms and their molecular control in mammalian-infective parasitic protozoa from the Excavata, Alveolata, and Amoebozoa supergroups, highlighting their often-underappreciated diversity and complexity. Billions of people and animals across the world are at risk from these pathogens, for which vaccines and/or optimal treatments are often not available. Exploiting the divergent cell division machinery in these parasites may provide new avenues for the treatment of protozoal disease.

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Section: Cytokinesis In the Amoebozoamentioning

confidence: 91%

Who Needs a Contractile Actomyosin Ring? The Plethora of Alternative Ways to Divide a Protozoan Parasite

Hammarton

2019

Front. Cell. Infect. Microbiol.

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“…GFP-myosin II [ 25 ], GFP-3ALA myosin II [ 24 ], GFP-E476K myosin II [ 25 ], GFP-Lifeact [ 18 ], GFP-MHCKC [ 26 ], GFP-PakA [ 27 ], GFP-dlpA [ 28 ], GFP-clathrin light chain [ 29 ], GFP-PTEN (G129E) [ 30 ], GFP-calmodulin [ 18 ], and Dd-GCaMP6s [ 31 ] expression vectors have been previously described. These expression vectors were transformed into cells by electroporation or laserporation, as described previously [ 32 , 33 ].…”

Section: Methodsmentioning

confidence: 99%

Dynamics of Myosin II Filaments during Wound Repair in Dividing Cells

Tanvir

Itoh

Adachi

et al. 2021

Cells

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Wound repair of cell membranes is essential for cell survival. Myosin II contributes to wound pore closure by interacting with actin filaments in larger cells; however, its role in smaller cells is unclear. In this study, we observed wound repair in dividing cells for the first time. The cell membrane in the cleavage furrow, where myosin II localized, was wounded by laserporation. Upon wounding, actin transiently accumulated, and myosin II transiently disappeared from the wound site. Ca2+ influx from the external medium triggered both actin and myosin II dynamics. Inhibition of calmodulin reduced both actin and myosin II dynamics. The wound closure time in myosin II-null cells was the same as that in wild-type cells, suggesting that myosin II is not essential for wound repair. We also found that disassembly of myosin II filaments by phosphorylation did not contribute to their disappearance, indicating a novel mechanism for myosin II delocalization from the cortex. Furthermore, we observed that several furrow-localizing proteins such as GAPA, PakA, myosin heavy chain kinase C, PTEN, and dynamin disappeared upon wounding. Herein, we discuss the possible mechanisms of myosin dynamics during wound repair.

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“…Dictyostelium cells have four modes of cytokinesis—cytokinesis A, B, C, and D [18,19,20,21]. Cytokinesis A depends on the contractile ring, cytokinesis B depends on the traction force of both the daughter cells, cytokinesis C is independent of cell cycle, and cytokinesis D is mediated by midwifery of other cells.…”

Section: Introductionmentioning

confidence: 99%

Dynamin-Like Protein B of Dictyostelium Contributes to Cytokinesis Cooperatively with Other Dynamins

Fujimoto

Tanaka

Rana

et al. 2019

Cells

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Dynamin is a large GTPase responsible for diverse cellular processes, such as endocytosis, division of organelles, and cytokinesis. The social amoebozoan, Dictyostelium discoideum, has five dynamin-like proteins: dymA, dymB, dlpA, dlpB, and dlpC. DymA, dlpA, or dlpB-deficient cells exhibited defects in cytokinesis. DlpA and dlpB were found to colocalize at cleavage furrows from the early phase, and dymA localized at the intercellular bridge connecting the two daughter cells, indicating that these dynamins contribute to cytokinesis at distinct dividing stages. Total internal reflection fluorescence microscopy revealed that dlpA and dlpB colocalized at individual dots at the furrow cortex. However, dlpA and dlpB did not colocalize with clathrin, suggesting that they are not involved in clathrin-mediated endocytosis. The fact that dlpA did not localize at the furrow in dlpB null cells and vice versa, as well as other several lines of evidence, suggests that hetero-oligomerization of dlpA and dlpB is required for them to bind to the furrow. The hetero-oligomers directly or indirectly associate with actin filaments, stabilizing them in the contractile rings. Interestingly, dlpA, but not dlpB, accumulated at the phagocytic cups independently of dlpB. Our results suggest that the hetero-oligomers of dlpA and dlpB contribute to cytokinesis cooperatively with dymA.

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Cytokinesis D is Mediated by Cortical Flow of Dividing Cells Instead of Chemotaxis

Cited by 11 publications

References 22 publications

Who Needs a Contractile Actomyosin Ring? The Plethora of Alternative Ways to Divide a Protozoan Parasite

Who Needs a Contractile Actomyosin Ring? The Plethora of Alternative Ways to Divide a Protozoan Parasite

Dynamics of Myosin II Filaments during Wound Repair in Dividing Cells

Dynamin-Like Protein B of Dictyostelium Contributes to Cytokinesis Cooperatively with Other Dynamins

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