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The CaMKII holoenzyme structure in activation-competent conformations

Author

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  • Janette B. Myers

    (Portland State University)

  • Vincent Zaegel

    (University of Colorado)

  • Steven J. Coultrap

    (University of Colorado)

  • Adam P. Miller

    (Portland State University)

  • K. Ulrich Bayer

    (University of Colorado)

  • Steve L. Reichow

    (Portland State University)

Abstract

The Ca2+/calmodulin-dependent protein kinase II (CaMKII) assembles into large 12-meric holoenzymes, which is thought to enable regulatory processes required for synaptic plasticity underlying learning, memory and cognition. Here we used single particle electron microscopy (EM) to determine a pseudoatomic model of the CaMKIIα holoenzyme in an extended and activation-competent conformation. The holoenzyme is organized by a rigid central hub complex, while positioning of the kinase domains is highly flexible, revealing dynamic holoenzymes ranging from 15–35 nm in diameter. While most kinase domains are ordered independently, ∼20% appear to form dimers and

Suggested Citation

  • Janette B. Myers & Vincent Zaegel & Steven J. Coultrap & Adam P. Miller & K. Ulrich Bayer & Steve L. Reichow, 2017. "The CaMKII holoenzyme structure in activation-competent conformations," Nature Communications, Nature, vol. 8(1), pages 1-15, August.
    • Handle: RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_ncomms15742
    DOI: 10.1038/ncomms15742
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