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© The Rockefeller University Press, 0022-1295/1999//555/ $5.00
Journal of General Physiology, Volume 113, Number 4, 1999

Article

Novel Gating Mechanism of Polyamine Block in the Strong Inward Rectifier K Channel Kir2.1

Jong-Kook Lee*, Scott A. John*, and James N. Weiss*,{ddagger}

From the UCLA Cardiovascular Research Laboratory, * Department of Medicine (Cardiology) and {ddagger} Department of Physiology, University of California, Los Angeles, School of Medicine, Los Angeles, California 90095

Inward rectifying K channels are essential for maintaining resting membrane potential and regulating excitability in many cell types. Previous studies have attributed the rectification properties of strong inward rectifiers such as Kir2.1 to voltage-dependent binding of intracellular polyamines or Mg to the pore (direct open channel block), thereby preventing outward passage of K ions. We have studied interactions between polyamines and the polyamine toxins philanthotoxin and argiotoxin on inward rectification in Kir2.1. We present evidence that high affinity polyamine block is not consistent with direct open channel block, but instead involves polyamines binding to another region of the channel (intrinsic gate) to form a blocking complex that occludes the pore. This interaction defines a novel mechanism of ion channel closure.

Key Words: spider venom toxin • polyamine • inward rectification • K channels

Address correspondence to James N. Weiss, M.D., Division of Cardiology, Rm 3641 MRL Building, UCLA School of Medicine, Los Angeles, CA 90095. Fax: 310-206-5777; E-mail: jweiss{at}mednet.ucla.edu


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