Publication: Phosphoinositide-binding proteins mark, shape and functionally modulate highly-diverged endocytic compartments in the parasitic protist Giardia lamblia
Phosphoinositide-binding proteins mark, shape and functionally modulate highly-diverged endocytic compartments in the parasitic protist Giardia lamblia
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Cernikova, L., Faso, C., & Hehl, A. B. (2020). Phosphoinositide-binding proteins mark, shape and functionally modulate highly-diverged endocytic compartments in the parasitic protist Giardia lamblia. PLoS Pathogens, 16(2), e1008317. https://doi.org/10.1371/journal.ppat.1008317
Abstract
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Abstract
Phosphorylated derivatives of phosphatidylinositol (PIPs) are key membrane lipid residues involved in clathrin-mediated endocytosis (CME). CME relies on PIP species PI(4,5)P2 to mark endocytic sites at the plasma membrane (PM) associated to clathrin-coated vesicle (CCV) formation. The highly diverged parasitic protist Giardia lamblia presents disordered and static clathrin assemblies at PM invaginations, contacting specialized endocytic organelles called peripheral vacuoles (PVs). The role for clathrin assemblies in fluid phase uptake
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- Cernikova, Lenka
- Faso, Carmen
- Hehl, Adrian B
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Cernikova, L., Faso, C., & Hehl, A. B. (2020). Phosphoinositide-binding proteins mark, shape and functionally modulate highly-diverged endocytic compartments in the parasitic protist Giardia lamblia. PLoS Pathogens, 16(2), e1008317. https://doi.org/10.1371/journal.ppat.1008317
