Multiple paralogues of α-SNAP in Giardia lamblia exhibit independent subcellular localization and redistribution during encystation and stress

Datta, Shankari Prasad; Jana, Kuladip; Mondal, Avisek; Ganguly, Subha; Sarkar, Soumalya

doi:10.1186/s13071-018-3112-1

Cited by 4 publications

(3 citation statements)

References 75 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Furthermore, the Gl PXD3 and Gl 15411 interactomes share proteins GL50803_16811 ( Gl 16811) tentatively annotated as a ZipA protein in GDB, and proteins GL50803_87677 ( Gl 87677) and GL50803_17060 ( Gl 17060), annotated as a NEK kinase and an ankyrin-domain carrying protein, respectively (Fig 6A). Unique interaction partners for Gl PXD3 include the SNARE protein Gl 7309 [44] and Gl NSF (GL50803_114776) [46]. In addition, protein GL50803_103709 carrying a predicted N-terminal BRO domain and protein GL50803_9605 were identified as unique Gl PXD3 interaction partners (Fig 6A).…”

Section: Resultsmentioning

confidence: 99%

Phosphoinositide-binding proteins mark, shape and functionally modulate highly-diverged endocytic compartments in the parasitic protistGiardia lamblia

Černíková

Faso

Hehl

2019

Preprint

View full text Add to dashboard Cite

Phosphorylated derivatives of phosphatidylinositol (PIPs), are key membrane lipid residues involved in clathrin-mediated endocytosis (CME). CME relies on 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 and their link to internal membranes via PIP-binding adaptors is unknown.Here we provide evidence for a robust link between clathrin assemblies and fluid-phase uptake in G. lamblia mediated by proteins carrying predicted PX, FYVE and NECAP1 PIP-binding modules. We show that chemical and genetic perturbation of PIP-residue binding and turnover elicits novel uptake and organelle-morphology phenotypes. A combination of co-immunoprecipitation and in silico annotation techniques expands the initial PIP-binding network with addition of new members. Our data indicate that, despite the partial conservation of lipid markers and protein cohorts known to play important roles in dynamic endocytic events in well-characterized model systems, the Giardia lineage presents a strikingly divergent clathrin-centered network. This includes several PIP-binding modules, often associated to domains of currently unknown function that shape and modulate fluid-phase uptake at PVs.

show abstract

Section: Resultsmentioning

confidence: 99%

Phosphoinositide-binding proteins mark, shape and functionally modulate highly-diverged endocytic compartments in the parasitic protistGiardia lamblia

Černíková

Faso

Hehl

2019

Preprint

View full text Add to dashboard Cite

show abstract

“…Therefore, we decided to evaluate the genes present in this signaling pathway with the same expression profile and found the coding gene for sec17. Sec17 is an a-SNAP protein belonging to SNARE proteins (soluble N-ethylmaleimide-sensitive factor adapting proteins receptors) related to intracellular trafficking in eukaryotes, such as trypanosomatids (Datta et al, 2018;Murungi et al, 2014). Analysis of the SNARE proteins in T. brucei has demonstrated their differential regulation during the life cycle of this parasite, indicating its importance in the differentiation of the parasite and thus explaining the differential expression profile observed here (Koumandou et al, 2008).…”

Section: Discussionmentioning

confidence: 98%

Transcriptomic changes across the life cycle of Trypanosoma cruzi II

Cruz-Saavedra

Vallejo

Guhl

et al. 2020

PeerJ

View full text Add to dashboard Cite

Trypanosoma cruzi is a flagellated protozoan that causes Chagas disease; it presents a complex life cycle comprising four morphological stages: epimastigote (EP), metacyclic trypomastigote (MT), cell-derived trypomastigote (CDT) and amastigote (AM). Previous transcriptomic studies on three stages (EPs, CDTs and AMs) have demonstrated differences in gene expressions among them; however, to the best of our knowledge, no studies have reported on gene expressions in MTs. Therefore, the present study compared differentially expressed genes (DEGs), and signaling pathway reconstruction in EPs, MTs, AMs and CDTs. The results revealed differences in gene expressions in the stages evaluated; these differences were greater between MTs and AMs-PTs. The signaling pathway that presented the highest number of DEGs in all the stages was associated with ribosomes protein profiles, whereas the other related pathways activated were processes related to energy metabolism from glucose, amino acid metabolism, or RNA regulation. However, the role of autophagy in the entire life cycle of T. cruzi and the presence of processes such as meiosis and homologous recombination in MTs (where the expressions of SPO11 and Rad51 plays a role) are crucial. These findings represent an important step towards the full understanding of the molecular basis during the life cycle of T. cruzi.

show abstract

“…Furthermore, the GlPXD3 and Gl15411 interactomes share proteins GL50803_16811 (Gl16811) tentatively annotated as a ZipA protein in GDB, and proteins GL50803_87677 (Gl87677) and GL50803_17060 (Gl17060), annotated as a NEK kinase and an ankyrin-domain carrying protein, respectively (Figs 4 and S4C). Unique interaction partners for GlPXD3 include the SNARE protein Gl7309 [47] and GlNSF (GL50803_114776) [49]. In addition, protein GL50803_103709 carrying a predicted N-terminal BRO domain and protein GL50803_9605 were identified as unique GlPXD3 interaction partners (Figs 4 and S4C).…”

Section: The Extended Interactomes Of Glpxd1 Glpxd4 and Glpxd6mentioning

confidence: 99%

Phosphoinositide-binding proteins mark, shape and functionally modulate highly-diverged endocytic compartments in the parasitic protist Giardia lamblia

2020

View full text Add to dashboard Cite

Phosphorylated derivatives of phosphatidylinositol (PIPs) are key membrane lipid residues involved in clathrin-mediated endocytosis (CME). CME relies on PIP species PI(4,5)P 2 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 and their link to internal membranes via PIP-binding adaptors is unknown. Here we provide evidence for a robust link between clathrin assemblies and fluid-phase uptake in G. lamblia mediated by proteins carrying predicted PX, FYVE and NECAP1 PIP-binding modules. We show that chemical and genetic perturbation of PIP-residue binding and turnover elicits novel uptake and organelle-morphology phenotypes. A combination of co-immunoprecipitation and in silico analysis techniques expands the initial PIP-binding network with addition of new members. Our data indicate that, despite the partial conservation of lipid markers and protein cohorts known to play important roles in dynamic endocytic events in well-characterized model systems, the Giardia lineage presents a strikingly divergent clathrin-centered network. This includes several PIP-binding modules, often associated to domains of currently unknown function that shape and modulate fluid-phase uptake at PVs.

show abstract

Multiple paralogues of α-SNAP in Giardia lamblia exhibit independent subcellular localization and redistribution during encystation and stress

Cited by 4 publications

References 75 publications

Phosphoinositide-binding proteins mark, shape and functionally modulate highly-diverged endocytic compartments in the parasitic protistGiardia lamblia

Phosphoinositide-binding proteins mark, shape and functionally modulate highly-diverged endocytic compartments in the parasitic protistGiardia lamblia

Transcriptomic changes across the life cycle of Trypanosoma cruzi II

Phosphoinositide-binding proteins mark, shape and functionally modulate highly-diverged endocytic compartments in the parasitic protist Giardia lamblia

Contact Info

Product

Resources

About