ArticleThe journal of physiological sciences : JPS2011
Inositol 1, 4, 5-trisphosphate receptor interacts with the SNARE domain of syntaxin 1B.
Article in The journal of physiological sciences : JPS, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
1 citing paper in PubMed, 2 citations in OpenAlex.
- Inositol 1,4,5-trisphosphate receptors and their protein partners as signalling hubs.The Journal of physiology · 2016Review
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Inositol 1, 4, 5-trisphosphate receptors (IP(3)Rs) are intracellular ligand-gated Ca(2+) channels that mediate Ca(2+) release from the endoplasmic reticulum (ER) into the cytosol and function in diverse cellular processes including fertilization, muscle contraction, apoptosis, secretion, and synaptic plasticity. The Ca(2+) release activity of IP(3)Rs is tightly regulated by many factors including IP(3)R-binding proteins. We show that IP(3)Rs interact with syntaxin 1 (Syx1), a membrane trafficking protein that regulates various plasma-membrane ion channels including N-, P/Q, and L-type voltage-gated Ca(2+) channels, voltage-gated potassium channels, and an epithelial sodium channel. We found that a SNARE-domain of Syx1B, one of the two Syx1 isoforms, directly interacted with the type1 IP(3)R (IP(3)R1) internal coupling domain, a known modulator for channel opening. These results indicate that Syx1B is an IP(3)R-interacting protein and that its interaction may play a crucial role in regulating the channel activity of IP(3)Rs in Syx1B-expressing cells.
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Registered trials
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