ArticleNature communications2022
Binary-FRET reveals transient excited-state structure associated with activity-dependent CaMKII - NR2B binding and adaptation.
Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 10 citations in OpenAlex.
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- Anomalous photophysical behaviors attributed to excitonic coupling in fluorescent proteins.Biophysical journal · 2025Article
- Decoding Molecular Network Dynamics in Cells: Advances in Multiplexed Live Imaging of Fluorescent Biosensors.Biosensors · 2025Review
- The treatment of myocardial ischemia-reperfusion injury: potential roles of natural drug modulating CaMKII.Frontiers in pharmacology · 2025Review
- Real-time single-molecule imaging of CaMKII-calmodulin interactions.Biophysical journal · 2024Article
- Structural insights into the disulfide isomerase and chaperone activity of TrbB of the F plasmid type IV secretion system.Current research in structural biology · 2024Article
- Molecular dynamics simulation analysis of structural dynamic cross correlation induced by odorant hydrogen-bonding in mouse eugenol ol- factory receptor.Biophysics and physicobiology · 2024Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Synaptic functions are mediated and modulated by a coordinated choreography of protein conformational changes and interactions in response to intracellular calcium dynamics. Time-lapse Förster resonance energy transfer can be used to study the dynamics of both conformational changes and protein-protein interactions simultaneously under physiological conditions if two resonance energy transfer reactions can be multiplexed. Binary-FRET is a technique developed to independently monitor the dynamics of calcium-calmodulin dependent protein kinase-II catalytic-domain pair separation in the holoenzyme, and its role in establishing activity-dependent holoenzyme affinity for the NR2B binding fragment of the N-methyl-D-aspartate receptor. Here we show that a transient excited-state intermediate exists where paired catalytic-domains in the holoenzyme first separate prior to subsequent NR2B association. Additionally, at non-saturating free calcium concentrations, our multiplexed approach reveals that the holoenzyme exhibits a biochemical form of plasticity, calcium dependent adaptation of T-site ligand binding affinity.
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