ArticleThe Biochemical journal2001
Effect of mutation of a calmodulin binding site on Ca2+ regulation of inositol trisphosphate receptors.
Article in The Biochemical journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 35 citations in OpenAlex.
- Non-Canonical Interaction between Calmodulin and Calcineurin Contributes to the Differential Regulation of Plant-Derived Calmodulins on Calcineurin.Journal of chemical information and modeling · 2021Article
- Structural basis for a hand-like site in the calcium sensor CatchER with fast kinetics.Acta crystallographica. Section D, Biological crystallography · 2013Article
- Activation of IP3 receptors requires an endogenous 1-8-14 calmodulin-binding motif.The Biochemical journal · 2013Article
- Inositol 1,4,5-trisphosphate receptor-mediated calcium release in Purkinje cells: from molecular mechanism to behavior.Cerebellum (London, England) · 2011Review
- IP(3) receptors: toward understanding their activation.Cold Spring Harbor perspectives in biology · 2010Review
- Regulation of IP(3)R Channel Gating by Ca(2+) and Ca(2+) Binding Proteins.Current topics in membranes · 2010Article
- Identification and dissection of Ca(2+)-binding sites in the extracellular domain of Ca(2+)-sensing receptor.The Journal of biological chemistry · 2007Article
- Inositol trisphosphate receptor Ca2+ release channels.Physiological reviews · 2007Review
- Modulation of mammalian inositol 1,4,5-trisphosphate receptor isoforms by calcium: a role of calcium sensor region.Biophysical journal · 2005Article
- Novel regulation of calcium inhibition of the inositol 1,4,5-trisphosphate receptor calcium-release channel.The Journal of general physiology · 2003Article
- Functional and biochemical analysis of the type 1 inositol (1,4,5)-trisphosphate receptor calcium sensor.Biophysical journal · 2003Article
- Localization and function of a calmodulin-apocalmodulin-binding domain in the N-terminal part of the type 1 inositol 1,4,5-trisphosphate receptor.The Biochemical journal · 2002Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Several studies have shown that calmodulin (CaM) modulates d-myo-inositol 1,4,5-trisphosphate (IP(3)) receptor (IP(3)R) channel activity and ligand binding to IP(3)Rs. It has been proposed that CaM may act as the Ca(2+) sensor for mediating Ca(2+) inhibition of IP(3)R channel activity. However, the functional role of CaM binding sites and the mechanism by which CaM regulates IP(3)R activities remains unclear. Tryptophan at position 1577 of type I IP(3)R has been shown to be part of a motif that is responsible for CaM binding to IP(3)Rs and we have mutated this residue to alanine in the long (neuronal) and short (peripheral) SII splice variants of the type I IP(3)R. CaM-Sepharose binding assays using COS-7 cell lysates confirmed that the W1577A mutant in both splice variants completely eliminated CaM binding. Functional measurements of IP(3)-mediated (45)Ca(2+) fluxes indicated that there was no change in the IP(3) sensitivity of the channel induced by the W1577A mutation. Such measurements also indicated that the W1577A mutants of both splice variants have a dependence on external [Ca(2+)] that was indistinguishable from the corresponding wild-types. Although subtle differences in the Ca(2+) and CaM sensitivity of [(3)H]IP(3) binding were noted between wild-type and mutant receptors, our data suggest that the CaM binding motif involving the W1577A locus does not play a role in Ca(2+) regulation of IP(3)R channel activity.
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