Binary-FRET reveals transient excited-state structure associated with activity-dependent CaMKII - NR2B binding and adaptation

Tuan A. Nguyen, Henry L. Puhl, Kirk Hines, Daniel J. Liput and Steven S. Vogel ()
Additional contact information
Tuan A. Nguyen: NIH
Henry L. Puhl: NIH
Kirk Hines: NIH
Daniel J. Liput: NIH
Steven S. Vogel: NIH

Nature Communications, 2022, vol. 13, issue 1, 1-14

Abstract: 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.

Date: 2022
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DOI: 10.1038/s41467-022-33795-8

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