ArticleEukaryotic cell2009
Dual acylation accounts for the localization of {alpha}19-giardin in the ventral flagellum pair of Giardia lamblia.
Article in Eukaryotic cell, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 24 citations in OpenAlex.
- Protein N-myristoylation: functions and mechanisms in control of innate immunity.Cellular & molecular immunology · 2021Review
- Article
- Differential protein expression and post-translational modifications in metronidazole-resistant Giardia duodenalis.GigaScience · 2018Article
- Dynamic protein S-palmitoylation mediates parasite life cycle progression and diverse mechanisms of virulence.Critical reviews in biochemistry and molecular biology · 2017Review
- Prokaryotic Expression ofBioMed research international · 2017Article
- Immunolocalization of α18- and α12-giardin in Giardia lamblia trophozoites.Parasitology research · 2016Article
- Identification of Giardia lamblia DHHC proteins and the role of protein S-palmitoylation in the encystation process.PLoS neglected tropical diseases · 2014Article
- Article
- Toxoplasma ISP4 is a central IMC sub-compartment protein whose localization depends on palmitoylation but not myristoylation.Molecular and biochemical parasitology · 2012Article
- Localization of retinitis pigmentosa 2 to cilia is regulated by Importin beta2.Journal of cell science · 2011Article
- A novel family of Toxoplasma IMC proteins displays a hierarchical organization and functions in coordinating parasite division.PLoS pathogens · 2010Article
- Article
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A Giardia-specific protein family denominated as alpha-giardins, represents the major protein component, besides tubulin, of the cytoskeleton of the human pathogenic parasite Giardia lamblia. One of its members, alpha19-giardin, carries an N-terminal sequence extension of MGCXXS, which in many proteins serves as a target for dual lipid conjugation: myristoylation at the glycine residue after removal of the methionine and palmitoylation at the cysteine residue. As the first experimental evidence of a lipid modification, we found alpha19-giardin to be associated with the membrane fraction of disrupted trophozoites. After heterologous coexpression of alpha19-giardin with giardial N-myristoyltransferase (NMT) in Escherichia coli, we found the protein in a myristoylated form. Additionally, after heterologous expression together with the palmitoyl transferase Pfa3 in Saccharomyces cerevisiae, alpha19-giardin associates with the membrane of the main vacuole. Immunocytochemical colocalization studies on wild-type Giardia trophozoites with tubulin provide evidence that alpha19-giardin exclusively localizes to the ventral pair of the giardial flagella. A mutant in which the putatively myristoylated N-terminal glycine residue was replaced by alanine lost this specific localization. Our findings suggest that the dual lipidation of alpha19-giardin is responsible for its specific flagellar localization.
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