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Structural basis of PIP2 activation of the classical inward rectifier K+ channel Kir2.2

Author

Listed:
  • Scott B. Hansen

    (Laboratory of Molecular Neurobiology & Biophysics, The Rockefeller University, Howard Hughes Medical Institute, 1230 York Avenue, New York, New York 10065, USA)

  • Xiao Tao

    (Laboratory of Molecular Neurobiology & Biophysics, The Rockefeller University, Howard Hughes Medical Institute, 1230 York Avenue, New York, New York 10065, USA)

  • Roderick MacKinnon

    (Laboratory of Molecular Neurobiology & Biophysics, The Rockefeller University, Howard Hughes Medical Institute, 1230 York Avenue, New York, New York 10065, USA)

Abstract

Inward rectifier potassium channels The regulatory lipid phosphatidylinositol 4,5-bisphosphate (PIP2) is the primary activator of inward rectifier K+ (Kir) channels. Kir channels control the resting membrane potential in a wide variety of excitable cells. The X-ray crystal structure of the Kir2.2 potassium channel in complex with a PIP2 derivative has now been determined. One PIP2 molecule binds to each of the four K+ channel subunits near the membrane inner leaflet. On binding, a large conformational change occurs, causing the cytoplasmic domain to engage the transmembrane domain and the pore to open. This work shows the structural basis for the regulation of receptors and ion channels by lipids, an important factor in the control of cell signalling.

Suggested Citation

  • Scott B. Hansen & Xiao Tao & Roderick MacKinnon, 2011. "Structural basis of PIP2 activation of the classical inward rectifier K+ channel Kir2.2," Nature, Nature, vol. 477(7365), pages 495-498, September.
    • Handle: RePEc:nat:nature:v:477:y:2011:i:7365:d:10.1038_nature10370
    DOI: 10.1038/nature10370
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    Cited by:

    1. Martina Nicoletti & Letizia Chiodo & Alessandro Loppini, 2021. "Biophysics and Modeling of Mechanotransduction in Neurons: A Review," Mathematics, MDPI, vol. 9(4), pages 1-32, February.
    2. Mengmeng Wang & Jing-Xiang Wu & Dian Ding & Lei Chen, 2022. "Structural insights into the mechanism of pancreatic KATP channel regulation by nucleotides," Nature Communications, Nature, vol. 13(1), pages 1-10, December.
    3. Camden M. Driggers & Yi-Ying Kuo & Phillip Zhu & Assmaa ElSheikh & Show-Ling Shyng, 2024. "Structure of an open KATP channel reveals tandem PIP2 binding sites mediating the Kir6.2 and SUR1 regulatory interface," Nature Communications, Nature, vol. 15(1), pages 1-16, December.
    4. Marcos Matamoros & Xue Wen Ng & Joshua B. Brettmann & David W. Piston & Colin G. Nichols, 2023. "Conformational plasticity of NaK2K and TREK2 potassium channel selectivity filters," Nature Communications, Nature, vol. 14(1), pages 1-12, December.
    5. Willow Coyote-Maestas & David Nedrud & Antonio Suma & Yungui He & Kenneth A. Matreyek & Douglas M. Fowler & Vincenzo Carnevale & Chad L. Myers & Daniel Schmidt, 2021. "Probing ion channel functional architecture and domain recombination compatibility by massively parallel domain insertion profiling," Nature Communications, Nature, vol. 12(1), pages 1-16, December.
    6. Grigory Maksaev & Michael Bründl-Jirout & Anna Stary-Weinzinger & Eva-Maria Zangerl-Plessl & Sun-Joo Lee & Colin G. Nichols, 2023. "Subunit gating resulting from individual protonation events in Kir2 channels," Nature Communications, Nature, vol. 14(1), pages 1-11, December.

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