ArticleProteins2009
Energetics of calmodulin domain interactions with the calmodulin binding domain of CaMKII.
Article in Proteins, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 42 citations in OpenAlex.
- Bidirectional coupling of neuronal CaRedox biology · 2026Article
- Neurogranin-MYH9 interaction regulates cytoskeletal remodeling in cerebral vasculature.Fluids and barriers of the CNS · 2025Article
- Nanoscale regulation of CaNature communications · 2022Article
- NaStructure (London, England : 1993) · 2021Article
- The CaeLife · 2021Article
- Structural basis of cytoplasmic NaV1.5 and NaV1.4 regulation.The Journal of general physiology · 2021Review
- Calmodulin binds to the N-terminal domain of the cardiac sodium channel NaChannels (Austin, Tex.) · 2020Article
- MICAL1 constrains cardiac stress responses and protects against disease by oxidizing CaMKII.The Journal of clinical investigation · 2020Article
- Neurogranin stimulates Ca2+/calmodulin-dependent kinase II by suppressing calcineurin activity at specific calcium spike frequencies.PLoS computational biology · 2020Article
- The S2-S3 Loop of Kv7.4 Channels Is Essential for Calmodulin Regulation of Channel Activation.Frontiers in physiology · 2020Article
- Non-Additive Effects of Binding Site Mutations in Calmodulin.Biochemistry · 2019Article
- CaNature communications · 2019Article
- A Calmodulin C-Lobe CaNeuron · 2018Article
- Biophysical analysis of the dynamics of calmodulin interactions with neurogranin and CaJournal of molecular recognition : JMR · 2017Article
- Defining potential roles of Pb(2+) in neurotoxicity from a calciomics approach.Metallomics : integrated biometal science · 2016Review
- Modulation of calmodulin lobes by different targets: an allosteric model with hemiconcerted conformational transitions.PLoS computational biology · 2015Article
- Reconstruction of Calmodulin Single-Molecule FRET States, Dye-Interactions, and CaMKII Peptide Binding by MultiNest and Classic Maximum Entropy.Chemical physics · 2013Article
- Substrate-selective and calcium-independent activation of CaMKII by α-actinin.The Journal of biological chemistry · 2012Article
- Lobe-specific functions of Ca2+·calmodulin in alphaCa2+·calmodulin-dependent protein kinase II activation.The Journal of biological chemistry · 2011Article
- Recognition of β-calcineurin by the domains of calmodulin: thermodynamic and structural evidence for distinct roles.Proteins · 2011Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Calmodulin (CaM) is an essential eukaryotic calcium receptor that regulates many kinases, including CaMKII. Calcium-depleted CaM does not bind to CaMKII under physiological conditions. However, binding of (Ca(2+))(4)-CaM to a basic amphipathic helix in CaMKII releases auto-inhibition of the kinase. The crystal structure of CaM bound to CaMKIIp, a peptide representing the CaM-binding domain (CaMBD) of CaMKII, shows an antiparallel interface: the C-domain of CaM primarily contacts the N-terminal half of the CaMBD. The two domains of calcium-saturated CaM are believed to play distinct roles in releasing auto-inhibition. To investigate the underlying mechanism of activation, calcium-dependent titrations of isolated domains of CaM binding to CaMKIIp were monitored using fluorescence anisotropy. The binding affinity of CaMKIIp for the domains of CaM increased upon saturation with calcium, with the C-domain having a 35-fold greater affinity than the N-domain. Because the interdomain linker of CaM regulates calcium-binding affinity and contribute to conformational change, the role of each CaM domain was explored further by investigating effects of CaMKIIp on site-knockout mutants affecting the calcium-binding sites of a single domain. Investigation of the thermodynamic linkage between saturation of individual calcium-binding sites and CaM-domain binding to CaMKIIp showed that calcium binding to Sites III and IV was sufficient to recapitulate the behavior of (Ca(2+))(4)-CaM. The magnitude of favorable interdomain cooperativity varied depending on which of the four calcium-binding sites were mutated, emphasizing differential regulatory roles for the domains of CaM, despite the high degree of homology among the four EF-hands of CaM.
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