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Articles de revues sur le sujet « IP3R3 »

Auteur : Grafiati

Publié le 9 mars 2023

Mis à jour le 31 juillet 2025

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1

Kochkina, Ekaterina N., Elizaveta Е. Kopylova, Olga A. Rogachevskaja, et al. "Agonist-Induced Ca2+ Signaling in HEK-293-Derived Cells Expressing a Single IP3 Receptor Isoform." Cells 13, no. 7 (2024): 562. http://dx.doi.org/10.3390/cells13070562.

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In mammals, three genes encode IP3 receptors (IP3Rs), which are involved in agonist-induced Ca2+ signaling in cells of apparently all types. Using the CRISPR/Cas9 approach for disruption of two out of three IP3R genes in HEK-293 cells, we generated three monoclonal cell lines, IP3R1-HEK, IP3R2-HEK, and IP3R3-HEK, with the single functional isoform, IP3R1, IP3R2, and IP3R3, respectively. All engineered cells responded to ACh with Ca2+ transients in an “all-or-nothing” manner, suggesting that each IP3R isotype was capable of mediating CICR. The sensitivity of cells to ACh strongly correlated wit

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Foulon, Arthur, Pierre Rybarczyk, Nicolas Jonckheere, et al. "Inositol (1,4,5)-Trisphosphate Receptors in Invasive Breast Cancer: A New Prognostic Tool?" International Journal of Molecular Sciences 23, no. 6 (2022): 2962. http://dx.doi.org/10.3390/ijms23062962.

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Breast cancer is the leading cause of cancer death among women in worldwide and France. The disease prognosis and treatment differ from one breast cancer subtype to another, and the disease outcome depends on many prognostic factors. Deregulation of ion flux (especially Ca2+ flux) is involved in many pathophysiology processes, including carcinogenesis. Inside the cell, the inositol-trisphosphate receptor (IP3R) is a major player in the regulation of the Ca2+ flux from the endoplasmic reticulum to the cytoplasm. The IP3Rs (and particularly the IP3R3 subtype) are known to be involved in prolifer

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Lee, Su Youn, Hee-Seop Yoo, Hye-Seung Choi, Ka Young Chung, and Min-Duk Seo. "Structural and dynamic insights into the subtype-specific IP3-binding mechanism of the IP3 receptor." Biochemical Journal 473, no. 20 (2016): 3533–43. http://dx.doi.org/10.1042/bcj20160539.

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There are three subtypes of vertebrate inositol 1,4,5-trisphosphate (IP3) receptor (IP3R), a Ca2+-release channel on the ER membrane — IP3R1, IP3R2, and IP3R3 — each of which has a distinctive role in disease development. To determine the subtype-specific IP3-binding mechanism, we compared the thermodynamics, thermal stability, and conformational dynamics between the N-terminal regions of IP3R1 (IP3R1-NT) and IP3R3 (IP3R3-NT) by performing circular dichroism (CD), isothermal titration calorimetry (ITC), and hydrogen–deuterium exchange mass spectrometry (HDX-MS). Previously determined crystal s

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NAGALEEKAR, VISWAS K., SEAN DIEHL, Ignacio Juncadella, et al. "Ets1-dependent IP3R3 expression in naïve CD4+ T cells is required for cytokine gene expression (87.22)." Journal of Immunology 178, no. 1_Supplement (2007): S132. http://dx.doi.org/10.4049/jimmunol.178.supp.87.22.

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Abstract IP3 receptors (IP3Rs) are critical for the release of Ca++ from intracellular stores in response to IP3 generated upon T cell receptor (TCR) ligation. However, little is known about the expression of the different IP3Rs in CD4+ T cells and their contribution to cytokine gene expression during antigen stimulation. Here, we show for the first time that prior to activation, naïve CD4+ T cells only express IP3R3, but not IP3R1 and IP3R2. IP3R3-mediated Ca++ flux for cytokine gene expression is required for an extended period of time on the order of hours that varies for specific cytokine

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Hytönen, Marjo K., Julius Rönkkö, Sruthi Hundi, et al. "IP3 receptor depletion in a spontaneous canine model of Charcot-Marie-Tooth disease 1J with amelogenesis imperfecta." PLOS Genetics 21, no. 1 (2025): e1011328. https://doi.org/10.1371/journal.pgen.1011328.

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Inositol 1,4,5-trisphosphate receptors (IP3R) mediate Ca2+ release from intracellular stores, contributing to complex regulation of numerous physiological responses. The involvement of the three IP3R genes (ITPR1, ITPR2 and ITPR3) in inherited human diseases has started to shed light on the essential roles of each receptor in different human tissues and cell types. Variants in the ITPR3 gene, which encodes IP3R3, have recently been found to cause demyelinating sensorimotor Charcot-Marie-Tooth neuropathy type 1J (CMT1J). In addition to peripheral neuropathy, immunodeficiency and tooth abnormali

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Khan, Samir A., Ana M. Rossi, Andrew M. Riley, Barry V. L. Potter, and Colin W. Taylor. "Subtype-selective regulation of IP3 receptors by thimerosal via cysteine residues within the IP3-binding core and suppressor domain." Biochemical Journal 451, no. 2 (2013): 177–84. http://dx.doi.org/10.1042/bj20121600.

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IP3R (IP3 [inositol 1,4,5-trisphosphate] receptors) and ryanodine receptors are the most widely expressed intracellular Ca2+ channels and both are regulated by thiol reagents. In DT40 cells stably expressing single subtypes of mammalian IP3R, low concentrations of thimerosal (also known as thiomersal), which oxidizes thiols to form a thiomercurylethyl complex, increased the sensitivity of IP3-evoked Ca2+ release via IP3R1 and IP3R2, but inhibited IP3R3. Activation of IP3R is initiated by IP3 binding to the IBC (IP3-binding core; residues 224–604) and proceeds via re-arrangement of an interface

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Kopylova, E. Е., I. S. Masulis, O. A. Rogachevskaja, et al. "Cellular Model for the Analysis of IRBIT-Dependent Regulation of the Type 1 IP<sub>3</sub> Receptor." Биологические мембраны Журнал мембранной и клеточной биологии 41, no. 1 (2024): 24–35. http://dx.doi.org/10.31857/s0233475524010023.

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In vertebrate genomes, three genes encode subunits of IP3 receptors, including IP3R1, IP3R2, and IP3R3. Despite high homology between different subunits, homotetrameric IP3 receptors formed by IP3R1, IP3R2, and IP₃R3 in the endoplasmic reticulum membrane are markedly distinct by their functional features and regulatory mechanisms. It was particularly reported that IP3R1 is specifically regulated by the IP3R binding protein released with IP₃ (IRBIT), which competes with IP3 for binding to IP3R1. In turn, affinity of IRBIT/IP₃R1 binding is regulated by phosphorylation of IRBIT. By using the CRIS

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HIROTA, Junji, Masashi BABA, Mineo MATSUMOTO, Teiichi FURUICHI, Kiyoshi TAKATSU, and Katsuhiko MIKOSHIBA. "T-cell-receptor signalling in inositol 1,4,5-trisphosphate receptor (IP3R) type-1-deficient mice: is IP3R type 1 essential for T-cell-receptor signalling?" Biochemical Journal 333, no. 3 (1998): 615–19. http://dx.doi.org/10.1042/bj3330615.

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Stimulation of T-cells via the T-cell receptor (TCR) complex is accompanied by an increase in intracellular Ca2+ concentration ([Ca2+]i). Recently, it was reported that a stable transformant of the human T-cell line, Jurkat, expressing an antisense cDNA construct of inositol 1,4,5-trisphosphate receptor (IP3R) type 1 (IP3R1), failed to demonstrate increased [Ca2+]i or interleukin-2 production after TCR stimulation and was also resistant to apoptotic stimuli. This cell line lacked IP3R1 expression, but expressed the type-2 and -3 receptors, IP3R2 and IP3R3 respectively [Jayaraman, Ondriasova, O

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Mikoshiba, Katsuhiko. "The IP3 receptor/Ca2+ channel and its cellular function." Biochemical Society Symposia 74 (January 12, 2007): 9–22. http://dx.doi.org/10.1042/bss2007c02.

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The IP3R [IP3 (inositol 1,4,5-trisphosphate) receptor] is responsible for Ca2+ release from the ER (endoplasmic reticulum). We have been working extensively on the P400 protein, which is deficient in Purkinje-neuron-degenerating mutant mice. We have discovered that P400 is an IP3R and we have determined the primary sequence. Purified IP3R, when incorporated into a lipid bilayer, works as a Ca2+ release channel and overexpression of IP3R shows enhanced IP3 binding and channel activity. Addition of an antibody blocks Ca2+ oscillations indicating that IP3R1 works as a Ca2+ oscillator. Studies on

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MORITA, Takao, Akihiko TANIMURA, Akihiro NEZU, Tomohiro KUROSAKI, and Yosuke TOJYO. "Functional analysis of the green fluorescent protein-tagged inositol 1,4,5-trisphosphate receptor type 3 in Ca2+ release and entry in DT40 B lymphocytes." Biochemical Journal 382, no. 3 (2004): 793–801. http://dx.doi.org/10.1042/bj20031970.

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We examined the function of GFP-IP3R3 (green fluorescent protein-tagged inositol 1,4,5-trisphosphate receptor type 3) in Ca2+ release and entry using a mutant DT40 cell line (IP3R-KO) in which all three IP3R genes had been disrupted. GFP-IP3R3 fluorescence largely overlapped with the distribution of endoplasmic reticulum, whereas a portion of GFP-IP3R3 apparently co-localized with the plasma membrane. The application of IP3 to permeabilized WT (wild-type) DT40 cells induced Ca2+ release from internal stores. Although this did not occur in IP3R-KO cells it was restored by expression of GFP-IP3R

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Yue, Lili, Liuqing Wang, Yangchun Du, et al. "Type 3 Inositol 1,4,5-Trisphosphate Receptor is a Crucial Regulator of Calcium Dynamics Mediated by Endoplasmic Reticulum in HEK Cells." Cells 9, no. 2 (2020): 275. http://dx.doi.org/10.3390/cells9020275.

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Being the largest the Ca2+ store in mammalian cells, endoplasmic reticulum (ER)-mediated Ca2+ signalling often involves both Ca2+ release via inositol 1, 4, 5-trisphosphate receptors (IP3R) and store operated Ca2+ entries (SOCE) through Ca2+ release activated Ca2+ (CRAC) channels on plasma membrane (PM). IP3Rs are functionally coupled with CRAC channels and other Ca2+ handling proteins. However, it still remains less well defined as to whether IP3Rs could regulate ER-mediated Ca2+ signals independent of their Ca2+ releasing ability. To address this, we generated IP3Rs triple and double knockou

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Song, Tengyao, Qiongyu Hao, Yun-Min Zheng, Qing-Hua Liu, and Yong-Xiao Wang. "Inositol 1,4,5-trisphosphate activates TRPC3 channels to cause extracellular Ca2+ influx in airway smooth muscle cells." American Journal of Physiology-Lung Cellular and Molecular Physiology 309, no. 12 (2015): L1455—L1466. http://dx.doi.org/10.1152/ajplung.00148.2015.

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Transient receptor potential-3 (TRPC3) channels play a predominant role in forming nonselective cation channels (NSCCs) in airway smooth muscle cells (ASMCs) and are significantly increased in their activity and expression in asthmatic ASMCs. To extend these novel findings, we have explored the regulatory mechanisms that control the activity of TRPC3 channels. Our data for the first time reveal that inositol 1,4,5-trisphosphate (IP3), an important endogenous signaling molecule, can significantly enhance the activity of single NSCCs in ASMCs. The analog of diacylglycerol (DAG; another endogenou

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BULTYNCK, Geert, Patrick DE SMET, Daniela ROSSI, et al. "Characterization and mapping of the 12kDa FK506-binding protein (FKBP12)-binding site on different isoforms of the ryanodine receptor and of the inositol 1,4,5-trisphosphate receptor." Biochemical Journal 354, no. 2 (2001): 413–22. http://dx.doi.org/10.1042/bj3540413.

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We investigated the interaction of the 12kDa FK506-binding protein (FKBP12) with two ryanodine-receptor isoforms (RyR1 and RyR3) and with two myo-inositol 1,4,5-trisphosphate (IP3) receptor isoforms (IP3R1 and IP3R3). Using glutathione S-transferase (GST)-FKBP12 affinity chromatography, we could efficiently extract RyR1 (42±7% of the solubilized RyR1) from terminal cisternae of skeletal muscle as well as RyR3 (32±4% of the solubilized RyR3) from RyR3-overexpressing HEK-293 cells. These interactions were completely abolished by FK506 (20µM) but were largely unaffected by RyR-channel modulators.

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Rahman, Taufiq. "Dynamic clustering of IP3 receptors by IP3." Biochemical Society Transactions 40, no. 2 (2012): 325–30. http://dx.doi.org/10.1042/bst20110772.

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The versatility of Ca2+ as an intracellular messenger stems largely from the impressive, but complex, spatiotemporal organization of the Ca2+ signals. For example, the latter when initiated by IP3 (inositol 1,4,5-trisphosphate) in many cells manifest hierarchical recruitment of elementary Ca2+ release events (‘blips’ and then ‘puffs’) en route to global regenerative Ca2+ waves as the cellular IP3 concentration rises. The spacing of IP3Rs (IP3 receptors) and their regulation by Ca2+ are key determinants of these spatially organized Ca2+ signals, but neither is adequately understood. IP3Rs have

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Bultynck, Geert, Daniela Rossi, Geert Callewaert, et al. "The Conserved Sites for the FK506-binding Proteins in Ryanodine Receptors and Inositol 1,4,5-Trisphosphate Receptors Are Structurally and Functionally Different." Journal of Biological Chemistry 276, no. 50 (2001): 47715–24. http://dx.doi.org/10.1074/jbc.m106573200.

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We compared the interaction of the FK506-binding protein (FKBP) with the type 3 ryanodine receptor (RyR3) and with the type 1 and type 3 inositol 1,4,5-trisphosphate receptor (IP3R1 and IP3R3), using a quantitative GST-FKBP12 and GST-FKBP12.6 affinity assay. We first characterized and mapped the interaction of the FKBPs with the RyR3. GST-FKBP12 as well as GST-FKBP12.6 were able to bind ∼30% of the solubilized RyR3. The interaction was completely abolished by FK506, strengthened by the addition of Mg2+, and weakened in the absence of Ca2+but was not affected by the addition of cyclic ADP-ribos

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BULTYNCK, Geert, Karolina SZLUFCIK, Nael Nadif KASRI, et al. "Thimerosal stimulates Ca2+ flux through inositol 1,4,5-trisphosphate receptor type 1, but not type 3, via modulation of an isoform-specific Ca2+-dependent intramolecular interaction." Biochemical Journal 381, no. 1 (2004): 87–96. http://dx.doi.org/10.1042/bj20040072.

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Thiol-reactive agents such as thimerosal have been shown to modulate the Ca2+-flux properties of IP3 (inositol 1,4,5-trisphosphate) receptor (IP3R) via an as yet unidentified mechanism [Parys, Missiaen, De Smedt, Droogmans and Casteels (1993) Pflügers Arch. 424, 516–522; Kaplin, Ferris, Voglmaier and Snyder (1994) J. Biol. Chem. 269, 28972–28978; Missiaen, Taylor and Berridge (1992) J. Physiol. (Cambridge, U.K.) 455, 623–640; Missiaen, Parys, Sienaert, Maes, Kunzelmann, Takahashi, Tanzawa and De Smedt (1998) J. Biol. Chem. 273, 8983–8986]. In the present study, we show that thimerosal potentia

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Piamsiri, Chanon, Nadezhda Fefelova, Sri Harika Pamarthi, et al. "Potential Roles of IP3 Receptors and Calcium in Programmed Cell Death and Implications in Cardiovascular Diseases." Biomolecules 14, no. 10 (2024): 1334. http://dx.doi.org/10.3390/biom14101334.

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Inositol 1,4,5-trisphosphate receptors (IP3Rs) play a crucial role in maintaining intracellular/cytosolic calcium ion (Ca2+i) homeostasis. The release of Ca2+ from IP3Rs serves as a second messenger and a modulatory factor influencing various intracellular and interorganelle communications during both physiological and pathological processes. Accumulating evidence from in vitro, in vivo, and clinical studies supports the notion that the overactivation of IP3Rs is linked to the pathogenesis of various cardiac conditions. The overactivation of IP3Rs results in the dysregulation of Ca2+ concentra

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VANLINGEN, Sara, Henk SIPMA, Patrick DE SMET, et al. "Ca2+ and calmodulin differentially modulate myo-inositol 1,4,5-trisphosphate (IP3)-binding to the recombinant ligand-binding domains of the various IP3 receptor isoforms." Biochemical Journal 346, no. 2 (2000): 275–80. http://dx.doi.org/10.1042/bj3460275.

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We have expressed the N-terminal 581 amino acids of type 1 myo-inositol 1,4,5-trisphosphate receptor (IP3R1), IP3R2 and IP3R3 as recombinant proteins [ligand-binding site 1 (lbs-1), lbs-2, lbs-3] in the soluble fraction of Escherichia coli. These recombinant proteins contain the complete IP3-binding domain and bound IP3 and adenophostin A with high affinity. Ca2+ and calmodulin were previously found to maximally inhibit IP3 binding to lbs-1 by 42±6 and 43±6% respectively, and with an IC50 of approx. 200 nM and 3 μM respectively [Sipma, De Smet, Sienaert, Vanlingen, Missiaen, Parys and De Smedt

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Pacher, Pál, Kumar Sharma, György Csordás, Yanqing Zhu та György Hajnóczky. "Uncoupling of ER-mitochondrial calcium communication by transforming growth factor-β". American Journal of Physiology-Renal Physiology 295, № 5 (2008): F1303—F1312. http://dx.doi.org/10.1152/ajprenal.90343.2008.

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Transforming growth factor-β (TGF-β) has been implicated as a key factor in mediating many cellular processes germane to disease pathogenesis, including diabetic vascular complications. TGF-β alters cytosolic [Ca2+] ([Ca2+]c) signals, which in some cases may result from the downregulation of the IP3 receptor Ca2+ channels (IP3R). Ca2+ released by IP3Rs is effectively transferred from endoplasmic reticulum (ER) to the mitochondria to stimulate ATP production and to allow feedback control of the Ca2+ mobilization. To assess the effect of TGF-β on the ER-mitochondrial Ca2+ transfer, we first stud

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Yuan, Zhaokan, Ting Cai, Jiang Tian, Alexander V. Ivanov, David R. Giovannucci, and Zijian Xie. "Na/K-ATPase Tethers Phospholipase C and IP3 Receptor into a Calcium-regulatory Complex." Molecular Biology of the Cell 16, no. 9 (2005): 4034–45. http://dx.doi.org/10.1091/mbc.e05-04-0295.

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We have shown that the caveolar Na/K-ATPase transmits ouabain signals via multiple signalplexes. To obtain the information on the composition of such complexes, we separated the Na/K-ATPase from the outer medulla of rat kidney into two different fractions by detergent treatment and density gradient centrifugation. Analysis of the light fraction indicated that both PLC-γ1 and IP3 receptors (isoforms 2 and 3, IP3R2 and IP3R3) were coenriched with the Na/K-ATPase, caveolin-1 and Src. GST pulldown assays revealed that the central loop of the Na/K-ATPase α1 subunit interacts with PLC-γ1, whereas th

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Liu, Yi, Xiaopin Ma, Hisashi Fujioka, Jun Liu, Shengdi Chen, and Xiongwei Zhu. "DJ-1 regulates the integrity and function of ER-mitochondria association through interaction with IP3R3-Grp75-VDAC1." Proceedings of the National Academy of Sciences 116, no. 50 (2019): 25322–28. http://dx.doi.org/10.1073/pnas.1906565116.

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Loss-of-function mutations in DJ-1 are associated with autosomal recessive early onset Parkinson’s disease (PD), yet the underlying pathogenic mechanism remains elusive. Here we demonstrate that DJ-1 localized to the mitochondria-associated membrane (MAM) both in vitro and in vivo. In fact, DJ-1 physically interacts with and is an essential component of the IP3R3-Grp75-VDAC1 complexes at MAM. Loss of DJ-1 disrupted the IP3R3-Grp75-VDAC1 complex and led to reduced endoplasmic reticulum (ER)-mitochondria association and disturbed function of MAM and mitochondria in vitro. These deficits could be

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Ren, Jun, Mingming Sun, Hao Zhou, et al. "FUNDC1 interacts with FBXL2 to govern mitochondrial integrity and cardiac function through an IP3R3-dependent manner in obesity." Science Advances 6, no. 38 (2020): eabc8561. http://dx.doi.org/10.1126/sciadv.abc8561.

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Defective mitophagy is causally linked to obesity complications. Here, we identified an interaction between mitophagy protein FUNDC1 (FUN14 domain containing 1) and receptor subunit of human SCF (SKP1/cullin/F-box protein) ubiquitin ligase complex FBXL2 as a gatekeeper for mitochondrial Ca2+ homeostasis through degradation of IP3R3 (inositol 1,4,5-trisphosphate receptor type 3). Loss of FUNDC1 in FUNDC1−/− mice accentuated high-fat diet–induced cardiac remodeling, functional and mitochondrial anomalies, cell death, rise in IP3R3, and Ca2+ overload. Mass spectrometry and co-immunoprecipitation

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Sundivakkam, Premanand C., Angela M. Kwiatek, Tiffany T. Sharma, Richard D. Minshall, Asrar B. Malik, and Chinnaswamy Tiruppathi. "Caveolin-1 scaffold domain interacts with TRPC1 and IP3R3 to regulate Ca2+ store release-induced Ca2+ entry in endothelial cells." American Journal of Physiology-Cell Physiology 296, no. 3 (2009): C403—C413. http://dx.doi.org/10.1152/ajpcell.00470.2008.

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Caveolin-1 (Cav-1) regulates agonist-induced Ca2+ entry in endothelial cells; however, how Cav-1 regulates this process is poorly understood. Here, we describe that Cav-1 scaffold domain (NH2-terminal residues 82–101; CSD) interacts with transient receptor potential canonical channel 1 (TRPC1) and inositol 1,4,5-trisphosphate receptor 3 (IP3R3) to regulate Ca2+ entry. We have shown previously that the TRPC1 COOH-terminal residues 781-789 bind to CSD. In the present study, we show that the TRPC1 COOH-terminal residues 781-789 truncated (TRPC1-CΔ781-789) mutant expression abolished Ca2+ store re

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Zhao, Guiling, Zachary P. Neeb, M. Dennis Leo, et al. "Type 1 IP3 receptors activate BKCa channels via local molecular coupling in arterial smooth muscle cells." Journal of General Physiology 136, no. 3 (2010): 283–91. http://dx.doi.org/10.1085/jgp.201010453.

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Plasma membrane large-conductance Ca2+-activated K+ (BKCa) channels and sarcoplasmic reticulum inositol 1,4,5-trisphosphate (IP3) receptors (IP3Rs) are expressed in a wide variety of cell types, including arterial smooth muscle cells. Here, we studied BKCa channel regulation by IP3 and IP3Rs in rat and mouse cerebral artery smooth muscle cells. IP3 activated BKCa channels both in intact cells and in excised inside-out membrane patches. IP3 caused concentration-dependent BKCa channel activation with an apparent dissociation constant (Kd) of ∼4 µM at physiological voltage (−40 mV) and intracellu

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Wolfram, Francis, Edward Morris, and Colin W. Taylor. "Three-dimensional structure of recombinant type 1 inositol 1,4,5-trisphosphate receptor." Biochemical Journal 428, no. 3 (2010): 483–89. http://dx.doi.org/10.1042/bj20100143.

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IP3Rs (inositol 1,4,5-trisphosphate receptors) are the intracellular channels that mediate release of Ca2+ from the endoplasmic reticulum in response to the many stimuli that evoke Ins(1,4,5)P3 formation. We characterized and purified type 1 IP3R heterologously expressed in Sf9 insect cells, and used the purified IP3R1 to determine its three-dimensional structure by electron microscopy and single-particle analysis. Recombinant IP3R1 has 4-fold symmetry with overall dimensions of approx. 19.5 nm×19.5 nm×17.5 nm. It comprises a small domain, which is likely to include the pore, linked by slender

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Zhao, Guiling, Adebowale Adebiyi, Eva Blaskova, Qi Xi, and Jonathan H. Jaggar. "Type 1 inositol 1,4,5-trisphosphate receptors mediate UTP-induced cation currents, Ca2+ signals, and vasoconstriction in cerebral arteries." American Journal of Physiology-Cell Physiology 295, no. 5 (2008): C1376—C1384. http://dx.doi.org/10.1152/ajpcell.00362.2008.

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Inositol 1,4,5-trisphosphate receptors (IP3Rs) regulate diverse physiological functions, including contraction and proliferation. There are three IP3R isoforms, but their functional significance in arterial smooth muscle cells is unclear. Here, we investigated relative expression and physiological functions of IP3R isoforms in cerebral artery smooth muscle cells. We show that 2-aminoethoxydiphenyl borate and xestospongin C, membrane-permeant IP3R blockers, reduced Ca2+ wave activation and global intracellular Ca2+ ([Ca2+]i) elevation stimulated by UTP, a phospholipase C-coupled purinergic rece

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Alzayady, Kamil J., and Richard J. H. Wojcikiewicz. "The role of Ca2+ in triggering inositol 1,4,5-trisphosphate receptor ubiquitination." Biochemical Journal 392, no. 3 (2005): 601–6. http://dx.doi.org/10.1042/bj20050949.

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The IP3R (inositol 1,4,5-trisphosphate receptor) forms tetrameric Ca2+ channels in ER (endoplasmic reticulum) membranes, where channel activity is largely under the control of the co-agonists IP3 and Ca2+. In cells stimulated using extracellular ligands that persistently elevate phosphoinositidase C activity, IP3Rs are rapidly ubiquitinated and then degraded by the proteasome through as yet undefined mechanisms. Whereas binding of IP3 has been suggested to be a key event in the triggering of IP3R ubiquitination the role of Ca2+ in this process remains unknown. In the present study we use αT3-1

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Yang, Yi-Dong, Man-Man Li, Gang Xu, et al. "Nogo-B Receptor Directs Mitochondria-Associated Membranes to Regulate Vascular Smooth Muscle Cell Proliferation." International Journal of Molecular Sciences 20, no. 9 (2019): 2319. http://dx.doi.org/10.3390/ijms20092319.

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Mitochondria-associated membranes (MAM) are a well-recognized contact link between the mitochondria and endoplasmic reticulum that affects mitochondrial biology and vascular smooth muscle cells (VSMCs) proliferation via the regulation of mitochondrial Ca2+(Ca2+m) influx. Nogo-B receptor (NgBR) plays a vital role in proliferation, epithelial-mesenchymal transition, and chemoresistance of some tumors. Recent studies have revealed that downregulation of NgBR, which stimulates the proliferation of VSMCs, but the underlying mechanism remains unclear. Here, we investigated the role of NgBR in MAM an

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Marongiu, Laura, Francesca Mingozzi, Clara Cigni, et al. "Inositol 1,4,5-trisphosphate 3-kinase B promotes Ca2+ mobilization and the inflammatory activity of dendritic cells." Science Signaling 14, no. 676 (2021): eaaz2120. http://dx.doi.org/10.1126/scisignal.aaz2120.

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Innate immune responses to Gram-negative bacteria depend on the recognition of lipopolysaccharide (LPS) by a receptor complex that includes CD14 and TLR4. In dendritic cells (DCs), CD14 enhances the activation not only of TLR4 but also that of the NFAT family of transcription factors, which suppresses cell survival and promotes the production of inflammatory mediators. NFAT activation requires Ca2+ mobilization. In DCs, Ca2+ mobilization in response to LPS depends on phospholipase C γ2 (PLCγ2), which produces inositol 1,4,5-trisphosphate (IP3). Here, we showed that the IP3 receptor 3 (IP3R3) a

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Meng, Xue-Lian, Hui-Ling Zhang, Lin-Lin Feng та ін. "Selenoprotein SelK increases the secretion of insulin from MIN6 β cells". RSC Advances 7, № 56 (2017): 35038–47. http://dx.doi.org/10.1039/c7ra05379g.

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Yu, Ting, Yun Wang, Dong Qian, et al. "Advanced Glycation End Products Impair Ca2+ Mobilization and Sensitization in Colonic Smooth Muscle Cells via the CAMP/PKA Pathway." Cellular Physiology and Biochemistry 43, no. 4 (2017): 1571–87. http://dx.doi.org/10.1159/000482005.

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Background/Aims: Excessive production of advanced glycation end products (AGEs) has been implicated in diabetes-related complications. This study aimed to investigate the mechanism by which AGEs potentially contribute to diabetes-associated colonic dysmotility. Methods: Control and streptozotocin (STZ)-induced diabetic groups were treated with aminoguanidine (AG). The colonic transit time and contractility of circular muscle strips was measured. ELISA, immunohistochemistry and western blotting were used to measure Nε-carboxymethyl-lysine (CML) levels. Primary cultured colonic smooth muscle cel

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Yamada, M., A. Miyawaki, K. Saito, et al. "The calmodulin-binding domain in the mouse type 1 inositol 1,4,5-trisphosphate receptor." Biochemical Journal 308, no. 1 (1995): 83–88. http://dx.doi.org/10.1042/bj3080083.

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We determined the amino acid sequence responsible for the calmodulin (CaM)-binding ability of mouse type 1 Ins(1,4,5)P3 receptor (IP3R1). We expressed various parts of IP3R1 from deleted cDNA and examined their CaM-binding ability. It was shown that the sequence stretching from Lys-1564 to Arg-1585 is necessary for the binding. The full-length IP3R1 with replacement of Trp-1576 by Ala lost its CaM-binding ability. Antibody against residues 1564-1585 of IP3R1 inhibited cerebellar IP3R1 from binding CaM. The fluorescence spectrum of the peptide that corresponds to residues 1564-1585 shifted when

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Marks, A. R. "Intracellular calcium-release channels: regulators of cell life and death." American Journal of Physiology-Heart and Circulatory Physiology 272, no. 2 (1997): H597—H605. http://dx.doi.org/10.1152/ajpheart.1997.272.2.h597.

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Intracellular Ca2+-release channels on the sarcoplasmic reticulum of striated muscle [ryanodine receptors (RyRs)] and on the endoplasmic reticulum of almost all types of cells [inositol 1,4,5-trisphosphate receptors (IP3Rs)] comprise a unique family of molecules that are structurally and functionally distinct from all other known ion channels. These channels play crucial roles in Ca2+-mediated signaling that triggers excitation-contraction coupling, T-lymphocyte activation, fertilization, and many other cellular functions. Three forms of RyR have been identified: RyR1, expressed predominantly

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Sun, Yi, Ana M. Rossi, Taufiq Rahman, and Colin W. Taylor. "Activation of IP3 receptors requires an endogenous 1-8-14 calmodulin-binding motif." Biochemical Journal 449, no. 1 (2012): 39–49. http://dx.doi.org/10.1042/bj20121034.

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Binding of IP3 (inositol 1,4,5-trisphosphate) to the IP3-binding core (residues 224–604) of IP3Rs (IP3 receptors) initiates opening of these ubiquitous intracellular Ca2+ channels. The mechanisms are unresolved, but require conformational changes to pass through the suppressor domain (residues 1–223). A calmodulin-binding peptide derived from myosin light chain kinase uncouples these events. We identified a similar conserved 1-8-14 calmodulin-binding motif within the suppressor domain of IP3R1 and, using peptides and mutagenesis, we demonstrate that it is essential for IP3R activation, whether

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Bononi, Angela, Carlotta Giorgi, Simone Patergnani, et al. "BAP1 regulates IP3R3-mediated Ca2+ flux to mitochondria suppressing cell transformation." Nature 546, no. 7659 (2017): 549–53. http://dx.doi.org/10.1038/nature22798.

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Liao, Chengheng, and Qing Zhang. "BBOX1 promotes triple-negative breast cancer progression by controlling IP3R3 stability." Molecular & Cellular Oncology 7, no. 6 (2020): 1813526. http://dx.doi.org/10.1080/23723556.2020.1813526.

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Ladenburger, Eva-Maria, Ivonne M. Sehring, Iris Korn, and Helmut Plattner. "Novel Types of Ca2+ Release Channels Participate in the Secretory Cycle of Paramecium Cells." Molecular and Cellular Biology 29, no. 13 (2009): 3605–22. http://dx.doi.org/10.1128/mcb.01592-08.

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ABSTRACT A database search of the Paramecium genome reveals 34 genes related to Ca2+-release channels of the inositol-1,4,5-trisphosphate (IP3) or ryanodine receptor type (IP3R, RyR). Phylogenetic analyses show that these Ca2+ release channels (CRCs) can be subdivided into six groups (Paramecium tetraurelia CRC-I to CRC-VI), each one with features in part reminiscent of IP3Rs and RyRs. We characterize here the P. tetraurelia CRC-IV-1 gene family, whose relationship to IP3Rs and RyRs is restricted to their C-terminal channel domain. CRC-IV-1 channels localize to cortical Ca2+ stores (alveolar s

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Tao, Rong, Chu-Pak Lau, and Gui-Rong Li. "Inositol 1,4,5-Trisphosphate Receptors Mediating Spontaneous Ca2+ Oscillation Favors Proliferation in Human Mesenchymal Stem Cells from Bone Marrow." Blood 108, no. 11 (2006): 2572. http://dx.doi.org/10.1182/blood.v108.11.2572.2572.

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Abstract Although human mesenchymal stem cells (hMSCs) constitute a very small population of cells in bone marrow, they play an important role in the regulation of hematopoietic microenvironment. The self-renew and/or proliferation of hMSCs is believed to be particularly important in maintaining bone marrow niche; however, the regulation of this process is not fully understood. The present study was designed to investigate whether spontaneous Ca2+ oscillation mediated by inositol 1,4,5-trisphosphate (IP3) receptors participates in the proliferation regulation in cultured hMSCs from bone marrow

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Kuchay, Shafi, Carlotta Giorgi, Daniele Simoneschi, et al. "PTEN counteracts FBXL2 to promote IP3R3- and Ca2+-mediated apoptosis limiting tumour growth." Nature 546, no. 7659 (2017): 554–58. http://dx.doi.org/10.1038/nature22965.

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Filadi, Riccardo, Nuno Santos Leal, Bernadette Schreiner, et al. "TOM70 Sustains Cell Bioenergetics by Promoting IP3R3-Mediated ER to Mitochondria Ca2+ Transfer." Current Biology 28, no. 3 (2018): 369–82. http://dx.doi.org/10.1016/j.cub.2017.12.047.

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Rosa, Nicolas, Hristina Ivanova, Larry E. Wagner, et al. "Bcl-xL acts as an inhibitor of IP3R channels, thereby antagonizing Ca2+-driven apoptosis." Cell Death & Differentiation 29, no. 4 (2021): 788–805. http://dx.doi.org/10.1038/s41418-021-00894-w.

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AbstractAnti-apoptotic Bcl-2-family members not only act at mitochondria but also at the endoplasmic reticulum, where they impact Ca2+ dynamics by controlling IP3 receptor (IP3R) function. Current models propose distinct roles for Bcl-2 vs. Bcl-xL, with Bcl-2 inhibiting IP3Rs and preventing pro-apoptotic Ca2+ release and Bcl-xL sensitizing IP3Rs to low [IP3] and promoting pro-survival Ca2+ oscillations. We here demonstrate that Bcl-xL too inhibits IP3R-mediated Ca2+ release by interacting with the same IP3R regions as Bcl-2. Via in silico superposition, we previously found that the residue K87

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Ye, Xiaolin, Meng Wang, Shantong Qiu, Yangyang Pan, Yan Cui, and Sijiu Yu. "Estradiol Alleviates Elevated Temperature-Induced Damage in Yak Oviductal Epithelial Cells by Maintaining Endoplasmic Reticulum Calciu Homeostasis." Animals 15, no. 9 (2025): 1305. https://doi.org/10.3390/ani15091305.

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Background: The oviduct is an organ that participates in multiple critical reproductive processes and provides essential nutritional support while maintaining a specialized microenvironment. It is particularly vulnerable to damage following heat stress-induced hyperthermia. Therefore, mitigating heat-induced damage to oviduct epithelial cells while preserving their physiological integrity under hyperthermia represents a critical therapeutic goal. Objective: This study aims to simulate the cellular damage state in yak oviduct epithelial cells (YOECs) under thermal challenge by increasing the in

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HIROTA, Junji, Hideaki ANDO, Kozo HAMADA, and Katsuhiko MIKOSHIBA. "Carbonic anhydrase-related protein is a novel binding protein for inositol 1,4,5-trisphosphate receptor type 1." Biochemical Journal 372, no. 2 (2003): 435–41. http://dx.doi.org/10.1042/bj20030110.

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The inositol 1,4,5-trisphosphate (IP3) receptor (IP3R) is an intracellular IP3-gated Ca2+ channel that is located on intracellular Ca2+ stores and modulates Ca2+ signalling. Using the yeast two-hybrid system, we screened a mouse brain cDNA library with bait constructs for mouse IP3R type 1 (IP3R1) to identify IP3R1-associated proteins. In this way, we found that carbonic anhydrase-related protein (CARP) is a novel IP3R1-binding protein. Western blot analysis revealed that CARP is expressed exclusively in Purkinje cells of the cerebellum, in which IP3R1 is abundantly expressed. Immunohistochemi

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Azumaya, Caleigh M., Emily A. Linton, Caitlin J. Risener, Terunaga Nakagawa, and Erkan Karakas. "Cryo-EM structure of human type-3 inositol triphosphate receptor reveals the presence of a self-binding peptide that acts as an antagonist." Journal of Biological Chemistry 295, no. 6 (2020): 1743–53. http://dx.doi.org/10.1074/jbc.ra119.011570.

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Calcium-mediated signaling through inositol 1,4,5-triphosphate receptors (IP3Rs) is essential for the regulation of numerous physiological processes, including fertilization, muscle contraction, apoptosis, secretion, and synaptic plasticity. Deregulation of IP3Rs leads to pathological calcium signaling and is implicated in many common diseases, including cancer and neurodegenerative, autoimmune, and metabolic diseases. Revealing the mechanism of activation and inhibition of this ion channel will be critical to an improved understanding of the biological processes that are controlled by IP3Rs.

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Vervliet, Tim, Jan B. Parys, and Geert Bultynck. "Bcl-2 and FKBP12 bind to IP3 and ryanodine receptors at overlapping sites: the complexity of protein–protein interactions for channel regulation." Biochemical Society Transactions 43, no. 3 (2015): 396–404. http://dx.doi.org/10.1042/bst20140298.

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The 12- and 12.6-kDa FK506-binding proteins, FKBP12 (12-kDa FK506-binding protein) and FKBP12.6 (12.6-kDa FK506-binding protein), have been implicated in the binding to and the regulation of ryanodine receptors (RyRs) and inositol 1,4,5-trisphosphate receptors (IP3Rs), both tetrameric intracellular Ca2+-release channels. Whereas the amino acid sequences responsible for FKBP12 binding to RyRs are conserved in IP3Rs, FKBP12 binding to IP3Rs has been questioned and could not be observed in various experimental models. Nevertheless, conservation of these residues in the different IP3R isoforms and

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Ye, Risheng, Min Ni, Miao Wang, et al. "Inositol 1,4,5-trisphosphate receptor 1 mutation perturbs glucose homeostasis and enhances susceptibility to diet-induced diabetes." Journal of Endocrinology 210, no. 2 (2011): 209–17. http://dx.doi.org/10.1530/joe-11-0012.

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The inositol 1,4,5-trisphosphate receptors (IP3Rs) as ligand-gated Ca2+ channels are key modulators of cellular processes. Despite advances in understanding their critical role in regulating neuronal function and cell death, how this family of proteins impact cell metabolism is just emerging. Unexpectedly, a transgenic mouse line (D2D) exhibited progressive glucose intolerance as a result of transgene insertion. Inverse PCR was used to identify the gene disruption in the D2D mice. This led to the discovery that Itpr1 is among the ten loci disrupted in chromosome 6. Itpr1 encodes for IP3R1, the

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Zhang, Dan, Michael J. Boulware, Matthew R. Pendleton, Taisaku Nogi, and Jonathan S. Marchant. "The inositol 1,4,5-trisphosphate receptor (Itpr) gene family in Xenopus: identification of type 2 and type 3 inositol 1,4,5-trisphosphate receptor subtypes." Biochemical Journal 404, no. 3 (2007): 383–91. http://dx.doi.org/10.1042/bj20070101.

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Studies in the Xenopus model system have provided considerable insight into the developmental role of intracellular Ca2+ signals produced by activation of IP3Rs (inositol 1,4,5-trisphosphate receptors). However, unlike mammalian systems where three IP3R subtypes have been well characterized, our molecular understanding of the IP3Rs that underpin Ca2+ signalling during Xenopus embryogenesis relate solely to the original characterization of the ‘Xenopus IP3R’ cloned and purified from Xenopus laevis oocytes several years ago. In the present study, we have identified Xenopus type 2 and type 3 IP3R

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Jia, Cuihong, and Colleen C. Hegg. "Effect of IP3R3 and NPY on age-related declines in olfactory stem cell proliferation." Neurobiology of Aging 36, no. 2 (2015): 1045–56. http://dx.doi.org/10.1016/j.neurobiolaging.2014.11.007.

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Kuchay, Shafi, Mohsan Saeed, Carlotta Giorgi, et al. "NS5A Promotes Constitutive Degradation of IP3R3 to Counteract Apoptosis Induced by Hepatitis C Virus." Cell Reports 25, no. 4 (2018): 833–40. http://dx.doi.org/10.1016/j.celrep.2018.09.088.

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Zhao, Yong, Jiezhang Li, Jinshuai Ma, Yijie Ding, Hongmei Fu, and Yiyu Zhang. "IP3R3 gene expression in laying duck tissues and its polymorphisms associated with eggshell quality." Gene 964 (September 2025): 149654. https://doi.org/10.1016/j.gene.2025.149654.

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