ArticleEukaryotic cell2008
Molecular identification of a SNAP-25-like SNARE protein in Paramecium.
Article in Eukaryotic cell, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 27 citations in OpenAlex.
- Calcium Ions as Conjugation-Specific Regulators inMicroorganisms · 2026Article
- Article
- Functions of the Plant Qbc SNARE SNAP25 in Cytokinesis and Biotic and Abiotic Stress Responses.Molecules and cells · 2020Article
- Phylogenetic Analysis of the vesicular fusion SNARE machinery revealing its functional divergence across Eukaryotes.Bioinformation · 2018Article
- GhSNAP33, a t-SNARE Protein FromFrontiers in plant science · 2018Article
- Functional Characterization of a Syntaxin Involved in Tomato (Frontiers in plant science · 2017Article
- Article
- A comparative analysis of trypanosomatid SNARE proteins.Parasitology international · 2014Article
- Expression of synaptosomal-associated protein-25 in the rat brain after subarachnoid hemorrhage.Neural regeneration research · 2013Article
- New insights into roles of acidocalcisomes and contractile vacuole complex in osmoregulation in protists.International review of cell and molecular biology · 2013Review
- Distinct subcellular localization of a group of synaptobrevin-like SNAREs in Paramecium tetraurelia and effects of silencing SNARE-specific chaperone NSF.Eukaryotic cell · 2010Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Using database searches of the completed Paramecium tetraurelia macronuclear genome with the metazoan SNAP-25 homologues, we identified a single 21-kDa Qb/c-SNARE in this ciliated protozoan, named P. tetraurelia SNAP (PtSNAP), containing the characteristic dual heptad repeat SNARE motifs of SNAP-25. The presence of only a single Qb/c class SNARE in P. tetraurelia is surprising in view of the multiple genome duplications and the high number of SNAREs found in other classes of this organism. As inferred from the subcellular localization of a green fluorescent protein (GFP) fusion construct, the protein is localized on a variety of intracellular membranes, and there is a large soluble pool of PtSNAP. Similarly, the PtSNAP that is detected with a specific antibody in fixed cells is associated with a number of intracellular membrane structures, including food vacuoles, the contractile vacuole system, and the sites of constitutive endo- and exocytosis. Surprisingly, using gene silencing, we could not assign a role to PtSNAP in the stimulated exocytosis of dense core vesicles (trichocysts), but we found an increased number of food vacuoles in PtSNAP-silenced cells. In conclusion, we identify PtSNAP as a Paramecium homologue of metazoan SNAP-25 that shows several divergent features, like resistance to cleavage by botulinum neurotoxins.
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