ArticleThe Journal of biological chemistry2013
Fragmented inositol 1,4,5-trisphosphate receptors retain tetrameric architecture and form functional Ca2+ release channels.
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 21 papers.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
21 citing papers in PubMed, 36 citations in OpenAlex.
- Monomethyl auristatin E and paclitaxel use different mechanisms to alter intracellular calcium signaling.Biochemical pharmacology · 2025Article
- Chemical Characterization and Biological Evaluation ofPlants (Basel, Switzerland) · 2023Article
- Missense mutations in inositol 1,4,5-trisphosphate receptor type 3 result in leaky CaiScience · 2022Article
- Conformational motions and ligand-binding underlying gating and regulation in IPNature communications · 2022Article
- Functional determination of calcium-binding sites required for the activation of inositol 1,4,5-trisphosphate receptors.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Disease-associated mutations in inositol 1,4,5-trisphosphate receptor subunits impair channel function.The Journal of biological chemistry · 2020Article
- Bcl-2-Protein Family as Modulators of IPCold Spring Harbor perspectives in biology · 2020Review
- Structure and Function of IPCold Spring Harbor perspectives in biology · 2019Review
- Differential regulation of ion channels function by proteolysis.Biochimica et biophysica acta. Molecular cell research · 2018Review
- 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
- Region-specific proteolysis differentially regulates type 1 inositol 1,4,5-trisphosphate receptor activity.The Journal of biological chemistry · 2017Article
- Proteolytic fragmentation of inositol 1,4,5-trisphosphate receptors: a novel mechanism regulating channel activity?The Journal of physiology · 2016Review
- Recessive and Dominant De Novo ITPR1 Mutations Cause Gillespie Syndrome.American journal of human genetics · 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
- Protein Fragmentation As a Regulatory Mechanism: Insights from Two Different CaFrontiers in physiology · 2016Article
- IP3R deficit underlies loss of salivary fluid secretion in Sjögren's Syndrome.Scientific reports · 2015Article
- Stable expression and function of the inositol 1,4,5-triphosphate receptor requires palmitoylation by a DHHC6/selenoprotein K complex.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Functional inositol 1,4,5-trisphosphate receptors assembled from concatenated homo- and heteromeric subunits.The Journal of biological chemistry · 2013Article
- The Bcl-2 protein family member Bok binds to the coupling domain of inositol 1,4,5-trisphosphate receptors and protects them from proteolytic cleavage.The Journal of biological chemistry · 2013Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Inositol 1,4,5-trisphosphate receptor isoforms are a family of ubiquitously expressed ligand-gated channels encoded by three individual genes. The proteins are localized to membranes of intracellular Ca(2+) stores and play pivotal roles in Ca(2+) homeostasis. Previous studies have demonstrated that IP3R1 is cleaved by the intracellular proteases calpain and caspase both in vivo and in vitro. However, the resultant cleavage products are poorly defined, and the functional consequences of these proteolytic events are not fully understood. We demonstrate that IP3R1 is cleaved during staurosporine-induced apoptosis, yielding N-terminal fragments encompassing the ligand-binding domain and the majority of the central modulatory domain together with a C-terminal fragment containing the channel domain and cytosolic tail. Notably, these fragments remain associated with the membrane after initiation of apoptotic cleavage. Furthermore, when recombinant IP3R1 fragments, corresponding to those predicted to be generated by caspase or calpain cleavage, are stably coexpressed in cells, they physically associate and form functional channels. These data provide novel insights regarding the regulation of IP3R1 during proteolysis and provide direct evidence that polypeptide continuity is not required for IP3R activation and Ca(2+) release.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.