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a spontaneous mutation of Itpr3 in a progenitor of the BTBR strain produces a heretofore unrecognized dysfunction of GPCR-mediated taste transduction
IP3R3 expressing microvillous cells are actively responsive to injury and promote recovery
KRAP physically interacts with IP3R1 (show ITPR1 Proteins) receptors in the kidney and IP3R3 receptors in the stomach.
The data suggested that that hair shedding is actively controlled by the IP3R3/NFAT (show NFATC1 Proteins)-dependent signaling pathway, possibly through the regulation of cytokeratin (show KRT4 Proteins) filaments in keratinocytes.
IP3R1 (show ITPR1 Proteins) and 3 are genetically redundant and essential for cardiovascular development; redundant roles of IP3R1 (show ITPR1 Proteins) and 3 may be implicated in regulation of cell death and the Mef2c (show MEF2C Proteins)-Smyd1 (show SMYD1 Proteins) transcriptional cascade during development of the second heart field
InsP3 receptors co-localize with ORAI calcium release-activated calcium modulator 1 (Orai1) channels in pancreatic acinar cells, even in IP3-deficient knockout mice.
These findings demonstrate that KRAP physically associates with IP(3)R (show ITPR1 Proteins) and regulates the proper localization of IP(3)R (show ITPR1 Proteins) in the epithelial cells in vivo and cultured cells.
The characterization of IP3R3 microvillous cells as non-neuronal chemoresponsive cells helps to explain the differing descriptions of microvillous cells in the literature.
Data demonstrate that a single aromatic residue in the suppressor domain (Tyr (show TYR Proteins)-167 in IP(3)R1 and Trp (show TYRP1 Proteins)-168 in IP(3)R3) plays a critical role in the coupling between ligand binding and channel gating.
Results strongly suggest that the Tyr (show TYR Proteins)-167 in IP(3)R1 and Trp (show TYRP1 Proteins)-168 in IP(3)R3 is critical for the functional coupling between IP(3) binding and channel gating.
Studies indicate that the ryanodine receptors (RyRs: RyR1, RyR2, RyR3) and inositol 1,4,5-trisphosphate receptors (IP3Rs: IP3R1 (show ITPR1 Proteins), IP3R2 (show ITPR2 Proteins), IP3R3) are the major Ca(2 (show CA2 Proteins)+) release channels (CRCs) on the endo/sarcoplasmic reticulum (ER/SR).
The transcription factor NRF2 (show GABPA Proteins) binds to the promoter of ITPR3 to inhibit its expression in cholangiocytes, leading to reduced calcium signaling and bile duct secretion.
miR (show MLXIP Proteins)-506 is a regulator of InsP3R3 expression and InsP3R3-mediated Ca2 (show CA2 Proteins)+ signaling and secretion.
The Galphaq (show GNAQ Proteins)-protein/coupled receptor/IP3R (show ITPR1 Proteins) axis modulates the electromechanical properties of the human myocardium and its propensity to develop arrhythmias.
A molecular and functional link between BKCa (show KCNMA1 Proteins) channel and IP3R3 in cancer cells as an important mechanism for tumor cell proliferation.
in human pulmonary fibroblasts, PDGF (show PDGFA Proteins) acts through IP3-induced Ca(2 (show CA2 Proteins)+)-release to trigger Ca(2 (show CA2 Proteins)+) waves, which in turn modulate gene expression of several matrix proteins.
Studies indicate that three subtypes of inositol 1,4,5-trisphosphate (IP3) receptors (IP3R1 (show ITPR1 Proteins), -2, and -3) are assembled to form homo- and heterotetrameric channels that mediate Ca(2 (show CA2 Proteins)+) release from intracellular stores.
The presence of isoform III of inositol 1,4,5-trisphosphate receptor is the key point of Akt (show AKT1 Proteins) activity on calcium-mediated apoptosis.
Ins (show INS Proteins)(1,4,5)P3R-mediated Ca2 (show CA2 Proteins)+ signaling was critical for starvation-induced autophagy stimulation.
The study provides biochemical evidence of the interaction between FKBP12 (show FKBP1A Proteins) and RYR1, RYR3 and IP3R (show ITPR1 Proteins).
role in cillary movement, coupled with chromogranin A (show CHGA Proteins)
This gene encodes a receptor for inositol 1,4,5-trisphosphate, a second messenger that mediates the release of intracellular calcium. The receptor contains a calcium channel at the C-terminus and the ligand-binding site at the N-terminus. Knockout studies in mice suggest that type 2 and type 3 inositol 1,4,5-trisphosphate receptors play a key role in exocrine secretion underlying energy metabolism and growth.
, IP3R 3
, inositol 1,4,5-trisphosphate receptor type 3
, type 3 InsP3 receptor
, type 3 inositol 1,4,5-trisphosphate receptor
, inositol 1,4,5-triphosphate receptor, type 3
, inositol 1,4,5-triphosphate receptor 3