Abstract
Inositol 1, 4, 5-trisphosphate receptors (IP3Rs) are intracellular ligand-gated Ca2+ channels that mediate Ca2+ 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 Ca2+ release activity of IP3Rs is tightly regulated by many factors including IP3R-binding proteins. We show that IP3Rs 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 IP3R (IP3R1) internal coupling domain, a known modulator for channel opening. These results indicate that Syx1B is an IP3R-interacting protein and that its interaction may play a crucial role in regulating the channel activity of IP3Rs in Syx1B-expressing cells. © 2011 The Physiological Society of Japan and Springer.
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Tanaka, S., Kabayama, H., Enomoto, M., Saito, N., & Mikoshiba, K. (2011). Inositol 1, 4, 5-trisphosphate receptor interacts with the SNARE domain of syntaxin 1B. Journal of Physiological Sciences, 61(3), 221–229. https://doi.org/10.1007/s12576-011-0140-4
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