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

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Listed:
  • Tuan A. Nguyen

    (NIH)

  • Henry L. Puhl

    (NIH)

  • Kirk Hines

    (NIH)

  • Daniel J. Liput

    (NIH)

  • Steven S. Vogel

    (NIH)

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.

Suggested Citation

  • Tuan A. Nguyen & Henry L. Puhl & Kirk Hines & Daniel J. Liput & Steven S. Vogel, 2022. "Binary-FRET reveals transient excited-state structure associated with activity-dependent CaMKII - NR2B binding and adaptation," Nature Communications, Nature, vol. 13(1), pages 1-14, December.
    • Handle: RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-33795-8
    DOI: 10.1038/s41467-022-33795-8
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    References listed on IDEAS

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    1. K.-Ulrich Bayer & Paul De Koninck & A. Soren Leonard & Johannes W. Hell & Howard Schulman, 2001. "Interaction with the NMDA receptor locks CaMKII in an active conformation," Nature, Nature, vol. 411(6839), pages 801-805, June.
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