ArticleACS chemical neuroscience2013
Calmodulin transduces Ca2+ oscillations into differential regulation of its target proteins.
Article in ACS chemical neuroscience, 2013. 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.
- Decoding ultrasensitive self-assembly of the calcium-regulated Tetrahymena cytoskeletal protein Tcb2 using optical actuation.The Journal of biological chemistry · 2025Article
- Decoding ultrasensitive self-assembly of the calcium-regulatedbioRxiv : the preprint server for biology · 2025Article
- Neurogranin modulates the rate of association between calmodulin and target peptides.Biophysical journal · 2024Article
- A Modeling and Analysis Study Reveals That CaMKII in Synaptic Plasticity Is a Dominant Affecter in CaM Systems in a T286 Phosphorylation-Dependent Manner.Molecules (Basel, Switzerland) · 2022Article
- Combined Pulsed Electron Double Resonance EPR and Molecular Dynamics Investigations of Calmodulin Suggest Effects of Crowding Agents on Protein Structures.Biochemistry · 2022Article
- Physiologically Relevant Free CaJournal of molecular biology · 2021Article
- Single cell protein analysis for systems biology.Essays in biochemistry · 2018Review
- Competitive Tuning Among CaCellular and molecular bioengineering · 2018Article
- Competitive tuning: Competition's role in setting the frequency-dependence of Ca2+-dependent proteins.PLoS computational biology · 2017Article
- Conserved properties of individual Ca2+-binding sites in calmodulin.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
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- Constant growth rate can be supported by decreasing energy flux and increasing aerobic glycolysis.Cell reports · 2014Article
- TRPV4-mediated mechanotransduction regulates the metabolic response of chondrocytes to dynamic loading.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
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Authors and funding
3 authors.
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Abstract
Diverse physiological processes are regulated differentially by Ca(2+) oscillations through the common regulatory hub calmodulin. The capacity of calmodulin to combine specificity with promiscuity remains to be resolved. Here we propose a mechanism based on the molecular properties of calmodulin, its two domains with separate Ca(2+) binding affinities, and target exchange rates that depend on both target identity and Ca(2+) occupancy. The binding dynamics among Ca(2+), Mg(2+), calmodulin, and its targets were modeled with mass-action differential equations based on experimentally determined protein concentrations and rate constants. The model predicts that the activation of calcineurin and nitric oxide synthase depends nonmonotonically on Ca(2+)-oscillation frequency. Preferential activation reaches a maximum at a target-specific frequency. Differential activation arises from the accumulation of inactive calmodulin-target intermediate complexes between Ca(2+) transients. Their accumulation provides the system with hysteresis and favors activation of some targets at the expense of others. The generality of this result was tested by simulating 60 000 networks with two, four, or eight targets with concentrations and rate constants from experimentally determined ranges. Most networks exhibit differential activation that increases in magnitude with the number of targets. Moreover, differential activation increases with decreasing calmodulin concentration due to competition among targets. The results rationalize calmodulin signaling in terms of the network topology and the molecular properties of calmodulin.
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