ArticleThe Journal of biological chemistry2013
Functional inositol 1,4,5-trisphosphate receptors assembled from concatenated homo- and heteromeric subunits.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed.
- Characterization of Immunolocalization of IP3R-1 in Skin Epithelium and its Changes in Non-Melanoma Skin Cancer: An Immuno-Histochemical and Clinical-Pathological Study.Indian dermatology online journal · 2026Article
- Missense mutations in inositol 1,4,5-trisphosphate receptor type 3 result in leaky CaiScience · 2022Article
- Location, location, and activation of a channel by calcium.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- CREB regulates the expression of type 1 inositol 1,4,5-trisphosphate receptors.Journal of cell science · 2021Article
- Disease-associated mutations in inositol 1,4,5-trisphosphate receptor subunits impair channel function.The Journal of biological chemistry · 2020Article
- Inositol 1,4,5-trisphosphate receptor type 3 plays a protective role in hepatocytes during hepatic ischemia-reperfusion injury.Cell calcium · 2020Article
- Covalent linkage of bacterial voltage-gated sodium channels.BMC biophysics · 2019Article
- All three IPScience signaling · 2018Article
- Redox regulation of type-I inositol trisphosphate receptors in intact mammalian cells.The Journal of biological chemistry · 2018Article
- Region-specific proteolysis differentially modulates type 2 and type 3 inositol 1,4,5-trisphosphate receptor activity in models of acute pancreatitis.The Journal of biological chemistry · 2018Article
- High expression of type I inositol 1,4,5-trisphosphate receptor in the kidney of rats with hepatorenal syndrome.World journal of gastroenterology · 2018Article
- The Making and Breaking of Inositol 1,4,5-Trisphosphate Receptor Tetramers.Messenger (Los Angeles, Calif. : Print) · 2018Article
- Region-specific proteolysis differentially regulates type 1 inositol 1,4,5-trisphosphate receptor activity.The Journal of biological chemistry · 2017Article
- PTEN counteracts FBXL2 to promote IP3R3- and CaNature · 2017Article
- Cardiac inositol 1,4,5-trisphosphate receptors.Biochimica et biophysica acta. Molecular cell research · 2017Review
- On the dynamical structure of calcium oscillations.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Proteolytic fragmentation of inositol 1,4,5-trisphosphate receptors: a novel mechanism regulating channel activity?The Journal of physiology · 2016Review
- IP3 receptors: Take four IP3 to open.Science signaling · 2016Article
- Defining the stoichiometry of inositol 1,4,5-trisphosphate binding required to initiate Ca2+ release.Science signaling · 2016Article
- Unique Regulatory Properties of Heterotetrameric Inositol 1,4,5-Trisphosphate Receptors Revealed by Studying Concatenated Receptor Constructs.The Journal of biological chemistry · 2016Article
Corrections and comments
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Authors and funding
8 authors.
Funding
Abstract
Vertebrate genomes code for three subtypes of inositol 1,4,5-trisphosphate (IP3) receptors (IP3R1, -2, and -3). Individual IP3R monomers are assembled to form homo- and heterotetrameric channels that mediate Ca(2+) release from intracellular stores. IP3R subtypes are regulated differentially by IP3, Ca(2+), ATP, and various other cellular factors and events. IP3R subtypes are seldom expressed in isolation in individual cell types, and cells often express different complements of IP3R subtypes. When multiple subtypes of IP3R are co-expressed, the subunit composition of channels cannot be specifically defined. Thus, how the subunit composition of heterotetrameric IP3R channels contributes to shaping the spatio-temporal properties of IP3-mediated Ca(2+) signals has been difficult to evaluate. To address this question, we created concatenated IP3R linked by short flexible linkers. Dimeric constructs were expressed in DT40-3KO cells, an IP3R null cell line. The dimeric proteins were localized to membranes, ran as intact dimeric proteins on SDS-PAGE, and migrated as an ∼1100-kDa band on blue native gels exactly as wild type IP3R. Importantly, IP3R channels formed from concatenated dimers were fully functional as indicated by agonist-induced Ca(2+) release. Using single channel "on-nucleus" patch clamp, the channels assembled from homodimers were essentially indistinguishable from those formed by the wild type receptor. However, the activity of channels formed from concatenated IP3R1 and IP3R2 heterodimers was dominated by IP3R2 in terms of the characteristics of regulation by ATP. These studies provide the first insight into the regulation of heterotetrameric IP3R of defined composition. Importantly, the results indicate that the properties of these channels are not simply a blend of those of the constituent IP3R monomers.
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