Mechanism of Cell Division in Entamoeba histolytica

Grewal, Jaspreet Singh; Lohia, Anuradha

doi:10.1007/978-4-431-55200-0_16

Cited by 4 publications

(5 citation statements)

References 41 publications

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“…Canonical molecular cell cycle checkpoints are often absent; some key cell cycle regulators are present, but their functions are not always conserved and they may act in conjunction with parasite-specific regulators. The level of molecular control is also variable, from minimal in Entamoeba (Mukherjee et al, 2009; Grewal and Lohia, 2015) to highly intricate with built-in flexibility in the kinetoplastids and apicomplexans. However, despite the physical and molecular differences compared to model organisms, some aspects of cytokinesis are conserved.…”

Section: Discussionmentioning

confidence: 99%

“…However, cell division is delinked from S phase and mitosis, occurring erratically and often asymmetrically, resulting in cells with no, one or multiple nuclei (Orozco et al, 1988; Lohia, 2003; Lohia et al, 2007; Mukherjee et al, 2009), with cell fusion events also contributing to multinuclear cell formation (Krishnan and Ghosh, 2018). Indeed, genome analysis suggests that E. histolytica encodes orthologs of all essential budding yeast cytokinesis proteins (although these have not been characterized), but that many cell cycle checkpoint proteins are not conserved (Grewal and Lohia, 2015), providing an explanation for the erratic division. Further, no actomyosin ring appears to be formed.…”

Section: Cytokinesis In the Amoebozoamentioning

confidence: 99%

“…(C) Dividing E. histolytica cells with an extended intercellular bridge. Adapted by permission from Springer Nature © (Grewal and Lohia, 2015).…”

Section: Cytokinesis In the Amoebozoamentioning

confidence: 99%

See 2 more Smart Citations

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: Discussionmentioning

confidence: 99%

Section: Cytokinesis In the Amoebozoamentioning

confidence: 99%

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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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“…Unfortunately, very little is known in E . histolytica except for the presence of a few homologs identified through sequence similarity searches [ 38 ]. Therefore, identification of EhCaBP6 as a potential cytokinesis and cell division regulating molecule is likely to help understand this complex process in this important parasite.…”

Section: Discussionmentioning

confidence: 99%

Structure of Ca2+-binding protein-6 from Entamoeba histolytica and its involvement in trophozoite proliferation regulation

et al. 2017

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Cell cycle of Entamoeba histolytica, the etiological agent of amoebiasis, follows a novel pathway, which includes nuclear division without the nuclear membrane disassembly. We report a nuclear localized Ca2+-binding protein from E. histolytica (abbreviated hereafter as EhCaBP6), which is associated with microtubules. We determined the 3D solution NMR structure of EhCaBP6, and identified one unusual, one canonical and two non-canonical cryptic EF-hand motifs. The cryptic EF-II and EF-IV pair with the Ca2+-binding EF-I and EF-III, respectively, to form a two-domain structure similar to Calmodulin and Centrin proteins. Downregulation of EhCaBP6 affects cell proliferation by causing delays in transition from G1 to S phase, and inhibition of DNA synthesis and cytokinesis. We also demonstrate that EhCaBP6 modulates microtubule dynamics by increasing the rate of tubulin polymerization. Our results, including structural inferences, suggest that EhCaBP6 is an unusual CaBP involved in regulating cell proliferation in E. histolytica similar to nuclear Calmodulin.

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“…More recently, MOB proteins were also detected and are conserved in other kinetoplastids, i.e., Trypanosoma rangeli, Trypanosoma cruzi, and Leishmania major [160,161] and in the fornicatan Giardia [162][163][164]. Conserved Mob1 genes have also been identified in Trichomonas vaginalis and Entamoeba histolytica, protozoans belonging to the phyla Parabasalia and Amoebozoa, respectively [165,166]. An analysis of the genome of the protozoan and obligate intracellular plant parasite Plasmodiophora brassicae also identified a conserved Mob1 gene [167].…”

Section: Non-alveolate Protozoamentioning

confidence: 99%

MOB: Pivotal Conserved Proteins in Cytokinesis, Cell Architecture and Tissue Homeostasis

Delgado

Carmona

Nolasco

et al. 2020

Biology

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The MOB family proteins are constituted by highly conserved eukaryote kinase signal adaptors that are often essential both for cell and organism survival. Historically, MOB family proteins have been described as kinase activators participating in Hippo and Mitotic Exit Network/ Septation Initiation Network (MEN/SIN) signaling pathways that have central roles in regulating cytokinesis, cell polarity, cell proliferation and cell fate to control organ growth and regeneration. In metazoans, MOB proteins act as central signal adaptors of the core kinase module MST1/2, LATS1/2, and NDR1/2 kinases that phosphorylate the YAP/TAZ transcriptional co-activators, effectors of the Hippo signaling pathway. More recently, MOBs have been shown to also have non-kinase partners and to be involved in cilia biology, indicating that its activity and regulation is more diverse than expected. In this review, we explore the possible ancestral role of MEN/SIN pathways on the built-in nature of a more complex and functionally expanded Hippo pathway, by focusing on the most conserved components of these pathways, the MOB proteins. We discuss the current knowledge of MOBs-regulated signaling, with emphasis on its evolutionary history and role in morphogenesis, cytokinesis, and cell polarity from unicellular to multicellular organisms.

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Mechanism of Cell Division in Entamoeba histolytica

Cited by 4 publications

References 41 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

Structure of Ca2+-binding protein-6 from Entamoeba histolytica and its involvement in trophozoite proliferation regulation

MOB: Pivotal Conserved Proteins in Cytokinesis, Cell Architecture and Tissue Homeostasis

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