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

Scott B. Hansen, Xiao Tao and Roderick MacKinnon ()
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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

Nature, 2011, vol. 477, issue 7365, 495-498

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.

Date: 2011
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DOI: 10.1038/nature10370

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