ArticleThe Journal of biological chemistry2010
Dissociation of calmodulin-target peptide complexes by the lipid mediator sphingosylphosphorylcholine: implications in calcium signaling.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 20 citations in OpenAlex.
- Review
- Can calmodulin bind to lipids of the cytosolic leaflet of plasma membranes?Open biology · 2024Article
- Sphingosylphosphorylcholine alleviates pressure overload-induced myocardial remodeling in mice via inhibiting CaM-JNK/p38 signaling pathway.Acta pharmacologica Sinica · 2024Article
- Structures of calmodulin-melittin complexes show multiple binding modes lacking classical anchoring interactions.The Journal of biological chemistry · 2023Article
- Assessing the Role of Calmodulin's Linker Flexibility in Target Binding.International journal of molecular sciences · 2021Article
- Structural resolution of switchable states of a de novo peptide assembly.Nature communications · 2021Article
- Light-Driven COFrontiers in molecular biosciences · 2021Article
- Comparison of ligand binding and conformational stability of human calmodulin with its homolog from the malaria parasiteFASEB bioAdvances · 2020Article
- Emerging roles of sphingosylphosphorylcholine in modulating cardiovascular functions and diseases.Acta pharmacologica Sinica · 2018Review
- The lipid mediator lysophosphatidic acid induces folding of disordered peptides with basic amphipathic character into rare conformations.Scientific reports · 2018Article
- Multicolor protein FRET with tryptophan, selective coumarin-cysteine labeling, and genetic acridonylalanine encoding.Chemical communications (Cambridge, England) · 2017Article
- Analytical methods for kinetic studies of biological interactions: A review.Journal of pharmaceutical and biomedical analysis · 2015Review
- Regulation of ryanodine receptors by sphingosylphosphorylcholine: involvement of both calmodulin-dependent and -independent mechanisms.Biochemical and biophysical research communications · 2010Article
- Structure and mechanism of calmodulin binding to a signaling sphingolipid reveal new aspects of lipid-protein interactions.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2010Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Previously we have identified the lipid mediator sphingosylphosphorylcholine (SPC) as the first potentially endogenous inhibitor of the ubiquitous Ca2+ sensor calmodulin (CaM) (Kovacs, E., and Liliom, K. (2008) Biochem. J. 410, 427-437). Here we give mechanistic insight into CaM inhibition by SPC, based on fluorescence stopped-flow studies with the model CaM-binding domain melittin. We demonstrate that both the peptide and SPC micelles bind to CaM in a rapid and reversible manner with comparable affinities. Furthermore, we present kinetic evidence that both species compete for the same target site on CaM, and thus SPC can be considered as a competitive inhibitor of CaM-target peptide interactions. We also show that SPC disrupts the complex of CaM and the CaM-binding domain of ryanodine receptor type 1, inositol 1,4,5-trisphosphate receptor type 1, and the plasma membrane Ca2+ pump. By interfering with these interactions, thus inhibiting the negative feedback that CaM has on Ca2+ signaling, we hypothesize that SPC could lead to Ca2+ mobilization in vivo. Hence, we suggest that the action of the sphingolipid on CaM might explain the previously recognized phenomenon that SPC liberates Ca2+ from intracellular stores. Moreover, we demonstrate that unlike traditional synthetic CaM inhibitors, SPC disrupts the complex between not only the Ca2+-saturated but also the apo form of the protein and the target peptide, suggesting a completely novel regulation for target proteins that constitutively bind CaM, such as ryanodine receptors.
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