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Evidence that the TRPV1 S1-S4 membrane domain contributes to thermosensing

Author

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  • Minjoo Kim

    (School of Molecular Sciences, Arizona State University
    The Biodesign Institute Virginia G. Piper Center for Personalized Diagnostics, Arizona State University)

  • Nicholas J. Sisco

    (School of Molecular Sciences, Arizona State University
    The Biodesign Institute Virginia G. Piper Center for Personalized Diagnostics, Arizona State University)

  • Jacob K. Hilton

    (School of Molecular Sciences, Arizona State University
    The Biodesign Institute Virginia G. Piper Center for Personalized Diagnostics, Arizona State University)

  • Camila M. Montano

    (The Biodesign Institute Virginia G. Piper Center for Personalized Diagnostics, Arizona State University)

  • Manuel A. Castro

    (School of Molecular Sciences, Arizona State University)

  • Brian R. Cherry

    (The Magnetic Resonance Research Center, Arizona State University)

  • Marcia Levitus

    (School of Molecular Sciences, Arizona State University
    The Biodesign Institute Center for Single Molecule Biophysics, Arizona State University)

  • Wade D. Van Horn

    (School of Molecular Sciences, Arizona State University
    The Biodesign Institute Virginia G. Piper Center for Personalized Diagnostics, Arizona State University)

Abstract

Sensing and responding to temperature is crucial in biology. The TRPV1 ion channel is a well-studied heat-sensing receptor that is also activated by vanilloid compounds, including capsaicin. Despite significant interest, the molecular underpinnings of thermosensing have remained elusive. The TRPV1 S1-S4 membrane domain couples chemical ligand binding to the pore domain during channel gating. Here we show that the S1-S4 domain also significantly contributes to thermosensing and couples to heat-activated gating. Evaluation of the isolated human TRPV1 S1-S4 domain by solution NMR, far-UV CD, and intrinsic fluorescence shows that this domain undergoes a non-denaturing temperature-dependent transition with a high thermosensitivity. Further NMR characterization of the temperature-dependent conformational changes suggests the contribution of the S1-S4 domain to thermosensing shares features with known coupling mechanisms between this domain with ligand and pH activation. Taken together, this study shows that the TRPV1 S1-S4 domain contributes to TRPV1 temperature-dependent activation.

Suggested Citation

  • Minjoo Kim & Nicholas J. Sisco & Jacob K. Hilton & Camila M. Montano & Manuel A. Castro & Brian R. Cherry & Marcia Levitus & Wade D. Van Horn, 2020. "Evidence that the TRPV1 S1-S4 membrane domain contributes to thermosensing," Nature Communications, Nature, vol. 11(1), pages 1-16, December.
    • Handle: RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-18026-2
    DOI: 10.1038/s41467-020-18026-2
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    Cited by:

    1. Emily G. Saccuzzo & Mubark D. Mebrat & Hailee F. Scelsi & Minjoo Kim & Minh Thu Ma & Xinya Su & Shannon E. Hill & Elisa Rheaume & Renhao Li & Matthew P. Torres & James C. Gumbart & Wade D. Van Horn & , 2024. "Competition between inside-out unfolding and pathogenic aggregation in an amyloid-forming β-propeller," Nature Communications, Nature, vol. 15(1), pages 1-14, December.

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