ArticleMicrobiologyOpen2019
Roles of end-binding 1 protein and gamma-tubulin small complex in cytokinesis and flagella formation of Giardia lamblia.
Article in MicrobiologyOpen, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 11 citations in OpenAlex.
- Two Centrins and Their Posttranslational Modification Modulate the Cell Cycle of Giardia lamblia.MicrobiologyOpen · 2025Article
- Kinesin-13, a Motor Protein, is Regulated by Polo-like Kinase in Giardia lamblia.The Korean journal of parasitology · 2022Article
- Efficient CRISPR/Cas9-mediated gene disruption in the tetraploid protistOpen biology · 2022Article
- A polo-like kinase modulates cytokinesis and flagella biogenesis in Giardia lamblia.Parasites & vectors · 2021Article
- Nek8445, a protein kinase required for microtubule regulation and cytokinesis inMolecular biology of the cell · 2020Article
- Microtubule organelles in Giardia.Advances in parasitology · 2020Review
- Roles of end-binding 1 protein and gamma-tubulin small complex in cytokinesis and flagella formation of Giardia lamblia.MicrobiologyOpen · 2019Article
- Role of gamma-giardin in ventral disc formation of Giardia lamblia.Parasites & vectors · 2019Article
- Who Needs a Contractile Actomyosin Ring? The Plethora of Alternative Ways to Divide a Protozoan Parasite.Frontiers in cellular and infection microbiology · 2019Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Giardia lamblia is a unicellular organism with two nuclei, a median body, eight flagella, and an adhesive disk. γ-Tubulin is a microtubule (MT)-nucleating protein that functions in the γ-tubulin small complex (γ-TuSC) in budding yeast. In this study, G. lamblia γ-tubulin (Glγ-tubulin) was found to bind to another MT-binding protein, namely G. lamblia end-binding protein 1 (GlEB1), via both in vivo and in vitro assays. Hemagglutinin (HA)-tagged Glγ-tubulin localized to the basal bodies, axonemes, and median bodies of G. lamblia trophozoites. The knockdown of Glγ-tubulin expression using an anti-Glγ-tubulin morpholino resulted in a decreased growth rate and an increased failed cytokinesis cells of Giardia. The formation of median bodies was affected, and the central pair of MTs in flagella was frequently missing in the Giardia treated with an anti-Glγ-tubulin morpholino. G. lamblia γ-tubulin complex protein 2 (GlGCP2) and GlGCP3, which are putative components of γ-TuSC, were co-immunoprecipitated with HA-tagged Glγ-tubulin in Giardia extracts. The knockdown of GlGCP2 and GlGCP3 expression also resulted in decreased formation of both the median body and flagella MTs. Knockdown of Glγ-tubulin, GlGCP2, and GlGCP3 expression affected localization of GlEB1 in G. lamblia. In addition, decreased level of GlEB1 caused reduced formation of median body and the central pair of flagella MTs. These results indicated that Glγ-tubulin plays a role in MT nucleation for median body formation and flagella biogenesis as a component of Glγ-TuSC in Giardia and GlEB1 may be involved in this process.
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