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A multigene family encoding R-SNAREs in the ciliate Paramecium tetraurelia. Traffic 7
, 2006
"... tor attachment protein receptors) mediate membrane interactions and are conventionally divided into Q-SNAREs and R-SNAREs according to the possession of a glutamine or arginine residue at the core of their SNARE domain. Here, we describe a set of R-SNAREs from the ciliate Paramecium tetraurelia cons ..."
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tor attachment protein receptors) mediate membrane interactions and are conventionally divided into Q-SNAREs and R-SNAREs according to the possession of a glutamine or arginine residue at the core of their SNARE domain. Here, we describe a set of R-SNAREs from the ciliate Paramecium tetraurelia consisting of seven families encoded by 12 genes that are expressed simultaneously. The complexity of the endomembrane system in Paramecium can explain this high number of genes. All P. tetraurelia synaptobrevins (PtSybs) possess a SNARE domain and show homology to the Longin family of R-SNAREs such as Ykt6, Sec22 and tetanus toxin-insensitive VAMP (TI-VAMP). We localized four exemplary PtSyb subfamilies with GFP constructs and antibodies on the light and electron microscopic level. PtSyb1-1, PtSyb1-2 and PtSyb3-1 were found in the endoplasmic reticulum, whereas PtSyb2 is localized exclusively in the contractile vacuole complex. PtSyb6 was found cytosolic but also resides in regularly arranged structures at the cell cortex (parasomal sacs), the cytoproct and oral apparatus, probably representing endocytotic compartments. With gene silencing, we showed that the R-SNARE of the contractile vacuole complex, PtSyb2, functions to maintain structural integrity as well as functionality of the osmoregulatory system but also affects cell division.
Novel Types of Ca 2 � Release Channels Participate in the Secretory Cycle of Paramecium Cells � †
, 2009
"... This article cites 107 articles, 42 of which can be accessed free ..."
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Cited by 6 (3 self)
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This article cites 107 articles, 42 of which can be accessed free
The vacuolar ATPase from Entamoeba histolytica: molecular cloning of the gene encoding for the B subunit and subcellular localization of the protein
- BMC Microbiol
, 2008
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"... Increases in the concentration of intracellular Ca2+, [Ca2+]i, govern a variety of processes in response to cell stimulation, such as exocytosis and cell contraction. A rise in intracellular Ca2+ may be due to Ca2+ influx from the outside medium or ..."
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Increases in the concentration of intracellular Ca2+, [Ca2+]i, govern a variety of processes in response to cell stimulation, such as exocytosis and cell contraction. A rise in intracellular Ca2+ may be due to Ca2+ influx from the outside medium or
unknown title
"... Increases in the concentration of intracellular Ca2+, [Ca2+]i, govern a variety of processes in response to cell stimulation, such as exocytosis and cell contraction. A rise in intracellular Ca2+ may be due to Ca2+ influx from the outside medium or ..."
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Increases in the concentration of intracellular Ca2+, [Ca2+]i, govern a variety of processes in response to cell stimulation, such as exocytosis and cell contraction. A rise in intracellular Ca2+ may be due to Ca2+ influx from the outside medium or
unknown title
"... Actin, an abundant cytoskeletal protein, is of paramount importance in forming the cell cortex, amoeboid movement, cyclosis, vesicle trafficking, cell division and for cell contraction etc. In the past few years, new aspects have ..."
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Actin, an abundant cytoskeletal protein, is of paramount importance in forming the cell cortex, amoeboid movement, cyclosis, vesicle trafficking, cell division and for cell contraction etc. In the past few years, new aspects have
Summary
, 2006
"... A broad spectrum of actin paralogs in Paramecium tetraurelia cells display differential localization and function ..."
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A broad spectrum of actin paralogs in Paramecium tetraurelia cells display differential localization and function
their Assignment to the Different Trafficking Pathways in Paramecium
"... These authors contributed equally to this work SNARE proteins have been classified as vesicular (v)- and target (t)-SNAREs and play a central role in the various membrane interactions in eukaryotic cells. Based on the Paramecium genome project, we have identified a multigene family of at least 26 me ..."
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These authors contributed equally to this work SNARE proteins have been classified as vesicular (v)- and target (t)-SNAREs and play a central role in the various membrane interactions in eukaryotic cells. Based on the Paramecium genome project, we have identified a multigene family of at least 26 members encoding the t-SNARE syntaxin (PtSyx) that can be grouped into 15 subfamilies. Paramecium syntaxins match the classical build-up of syntaxins, being ‘tail-anchored ’ membrane proteins with an N-terminal cytoplasmic domain and a membranebound single C-terminal hydrophobic domain. The membrane anchor is preceded by a conserved SNARE domain of 60 amino acids that is supposed to participate in SNARE complex assembly. In a phylogenetic analysis, most of the Paramecium syntaxin genes were found to cluster in groups together with those from other organisms in a pathway-specific manner, allowing an assignment to different compartments in a homology-dependent way. However, some of them seem to have no counterparts in metazoans. In another approach, we fused one representative member of each of the syntaxin isoforms to green fluorescent protein and assessed the in vivo localization, which was further supported by immunolocalization of some syntaxins. This allowed us to assign syntaxins to all important trafficking pathways in Paramecium.
with the osmoregulatory system
, 2006
"... In the ciliate Paramecium, a variety of well characterized processes are regulated by Ca2+, e.g. exocytosis, endocytosis and ciliary beat. Therefore, among protozoa, Paramecium is considered a model organism for Ca2+ signaling, although the molecular identity of the channels responsible for the Ca2+ ..."
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In the ciliate Paramecium, a variety of well characterized processes are regulated by Ca2+, e.g. exocytosis, endocytosis and ciliary beat. Therefore, among protozoa, Paramecium is considered a model organism for Ca2+ signaling, although the molecular identity of the channels responsible for the Ca2+ signals remains largely unknown. We have cloned – for the first time in a protozoan – the full sequence of the gene encoding a putative inositol (1,4,5)trisphosphate (Ins(1,4,5)P3) receptor from Paramecium tetraurelia cells showing molecular characteristics of higher eukaryotic cells. The homologously expressed Ins(1,4,5)P3binding domain binds [ 3 Summary H]Ins(1,4,5)P3, whereas antibodies unexpectedly localize this protein to the osmoregulatory system. The level of Ins(1,4,5)P3-receptor expression was reduced, as shown on a transcriptional level and by immuno-staining, by decreasing the concentration of
