ArticleThe Biochemical journal2002
Localization and function of a calmodulin-apocalmodulin-binding domain in the N-terminal part of the type 1 inositol 1,4,5-trisphosphate receptor.
Article in The Biochemical journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 76 citations in OpenAlex.
- Structure-Function Diversity of Calcium-Binding Proteins (CaBPs): Key Roles in Cell Signalling and Disease.Cells · 2025Review
- Calmodulin Mutations in Human Disease.Channels (Austin, Tex.) · 2023Review
- Conformational motions and ligand-binding underlying gating and regulation in IPNature communications · 2022Article
- Structural Characterization of Carbonic Anhydrase VIII and Effects of Missense Single Nucleotide Variations to Protein Structure and Function.International journal of molecular sciences · 2020Article
- Exploration of inositol 1,4,5-trisphosphate (IPScientific reports · 2019Article
- The lipid mediator lysophosphatidic acid induces folding of disordered peptides with basic amphipathic character into rare conformations.Scientific reports · 2018Article
- IPCellular and molecular life sciences : CMLS · 2017Review
- The knottin-like Blufensin family regulates genes involved in nuclear import and the secretory pathway in barley-powdery mildew interactions.Frontiers in plant science · 2015Article
- Activation of IP3 receptors requires an endogenous 1-8-14 calmodulin-binding motif.The Biochemical journal · 2013Article
- IP(3) receptors: toward understanding their activation.Cold Spring Harbor perspectives in biology · 2010Review
- Unraveling the role of polycystin-2/inositol 1,4,5-trisphosphate receptor interaction in Ca signaling.Communicative & integrative biology · 2010Article
- Calcium-dependent conformational changes in inositol trisphosphate receptors.The Journal of biological chemistry · 2010Article
- Dissociation of calmodulin-target peptide complexes by the lipid mediator sphingosylphosphorylcholine: implications in calcium signaling.The Journal of biological chemistry · 2010Article
- Regulation of inositol 1,4,5-trisphosphate-induced Ca2+ release by reversible phosphorylation and dephosphorylation.Biochimica et biophysica acta · 2009Review
- Regulation of Ca2+ signaling with particular focus on mast cells.Critical reviews in immunology · 2009Review
- Protein phosphatase-1 is a novel regulator of the interaction between IRBIT and the inositol 1,4,5-trisphosphate receptor.The Biochemical journal · 2007Article
- Inositol trisphosphate receptor Ca2+ release channels.Physiological reviews · 2007Review
- 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.The Biochemical journal · 2004Article
- Regulation of InsP3 receptor activity by neuronal Ca2+-binding proteins.The EMBO journal · 2004Article
- Single channel function of inositol 1,4,5-trisphosphate receptor type-1 and -2 isoform domain-swap chimeras.The Journal of general physiology · 2003Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Calmodulin (CaM) is a ubiquitous protein that plays a critical role in regulating cellular functions by altering the activity of a large number of proteins, including the d-myo-inositol 1,4,5-trisphosphate (IP3) receptor (IP3R). CaM inhibits IP3 binding in both the presence and absence of Ca2+ and IP3-induced Ca2+ release in the presence of Ca2+. We have now mapped and characterized a Ca2+-independent CaM-binding site in the N-terminal part of the type 1 IP3R (IP3R1). This site could be responsible for the inhibitory effects of CaM on IP3 binding. We therefore expressed the N-terminal 581 amino acids of IP3R1 as a His-tagged recombinant protein, containing the functional IP3-binding pocket. We showed that CaM, both in the presence and absence of Ca2+, inhibited IP3 binding to this recombinant protein with an IC50 of approx. 2 microM. Deletion of the N-terminal 225 amino acids completely abolished the effects of both Ca2+ and CaM on IP3 binding. We mapped the Ca2+-independent CaM-binding site to a recombinant glutathione S-transferase fusion protein containing the first 159 amino acids of IP3R1 and then made different synthetic peptides overlapping this region. We demonstrated that two synthetic peptides matching amino acids 49-81 and 106-128 bound CaM independently of Ca2+ and could reverse the inhibition of IP3 binding caused by CaM. This suggests that these sequences are components of a discontinuous Ca2+-independent CaM-binding domain, which is probably involved in the inhibition of IP3 binding by CaM.
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