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Editing of human KV1.1 channel mRNAs disrupts binding of the N-terminus tip at the intracellular cavity

Author

Listed:
  • Carlos Gonzalez

    (Centro Interdisciplinario de Neurociencia de Valparaiso, Universidad de Valparaiso)

  • Angelica Lopez-Rodriguez

    (Molecular Neurophysiology Section, Porter Neuroscience Research Center, National Institute of Neurological Disorders and Stroke, National Institutes of Health)

  • Deepa Srikumar

    (Molecular Neurophysiology Section, Porter Neuroscience Research Center, National Institute of Neurological Disorders and Stroke, National Institutes of Health)

  • Joshua J.C. Rosenthal

    (Institute of Neurobiology, University of Puerto Rico-Medical Sciences Campus
    Department of Biochemistry,University of Puerto Rico-Medical Sciences Campus)

  • Miguel Holmgren

    (Molecular Neurophysiology Section, Porter Neuroscience Research Center, National Institute of Neurological Disorders and Stroke, National Institutes of Health)

Abstract

In the nervous system, A→I RNA editing has an important role in regulating neuronal excitability. Ligand-gated membrane receptors, synaptic proteins, as well as ion channels, are targets for recoding by RNA editing. Although scores of editing sites have been identified in the mammalian brain, little is known about the functional alterations that they cause, and even less about the mechanistic underpinnings of how they change protein function. We have previously shown that an RNA editing event (I400 V) alters the inner permeation pathway of human KV1.1, modifying the kinetics of fast inactivation. Here we show that the channel's inactivation gate enters deep into the ion permeation pathway and the very tip establishes a direct hydrophobic interaction with the edited position. By converting I to V, the intimacy of the interaction is reduced, allowing the inactivation gate to unbind with much faster kinetics.

Suggested Citation

  • Carlos Gonzalez & Angelica Lopez-Rodriguez & Deepa Srikumar & Joshua J.C. Rosenthal & Miguel Holmgren, 2011. "Editing of human KV1.1 channel mRNAs disrupts binding of the N-terminus tip at the intracellular cavity," Nature Communications, Nature, vol. 2(1), pages 1-6, September.
    • Handle: RePEc:nat:natcom:v:2:y:2011:i:1:d:10.1038_ncomms1446
    DOI: 10.1038/ncomms1446
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    Cited by:

    1. Shubhangi Agarwal & Elizabeth D. Kim & Sangyun Lee & Alexander Simon & Alessio Accardi & Crina M. Nimigean, 2025. "Ball-and-chain inactivation of a human large conductance calcium-activated potassium channel," Nature Communications, Nature, vol. 16(1), pages 1-14, December.

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