| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
Biophysical Journal 70: 754-761 (1996)
© 1996 the Biophysical Society
Department of Physiology, University of California, San Francisco 94143-0724, USA.
ABSTRACT
Inwardly rectifying K+ channels are highly selective for K+ ions and show strong interaction with ions in the pore. Both features are important for the physiological functions of these channels and pose intriguing mechanistic questions of ion permeation. The aspartate residue in the second putative transmembrane segment of the IRK1 inwardly rectifying K+ channel, previously implicated in inward rectification gating due to cytoplasmic Mg2+ and polyamine block, is found in this study to be crucial for the channel's ability to distinguish between K+ and Rb+ ions. Mutation of this residue also perturbs the interaction between the channel pore and the Sr2+ blocking ion. Our studies suggest that this aspartate residue contributes to a selectivity filter near the cytoplasmic end of the pore.
This article has been cited by other articles:
 |
|
 |
|
  N. D'Avanzo, H. C. Cho, I. Tolokh, R. Pekhletski, I. Tolokh, C. Gray, S. Goldman, and P. H. Backx Conduction through the Inward Rectifier Potassium Channel, Kir2.1, Is Increased by Negatively Charged Extracellular Residues J. Gen. Physiol., April 25, 2005; 125(5): 493 - 503. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 D. Bichet, Y.-F. Lin, C. A. Ibarra, C. S. Huang, B. A. Yi, Y. N. Jan, and L. Y. Jan Evolving potassium channels by means of yeast selection reveals structural elements important for selectivity PNAS, March 30, 2004; 101(13): 4441 - 4446. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 N. Alagem, S. Yesylevskyy, and E. Reuveny The Pore Helix Is Involved in Stabilizing the Open State of Inwardly Rectifying K+ Channels Biophys. J., July 1, 2003; 85(1): 300 - 312. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 S. Sheng, K. A. McNulty, J. M. Harvey, and T. R. Kleyman Second Transmembrane Domains of ENaC Subunits Contribute to Ion Permeation and Selectivity J. Biol. Chem., November 16, 2001; 276(47): 44091 - 44098. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 A. L. B. Langloh, B. Berdiev, H.-L. Ji, K. Keyser, B. A. Stanton, and D. J. Benos Charged residues in the M2 region of alpha -hENaC play a role in channel conductance Am J Physiol Cell Physiol, February 1, 2000; 278(2): C277 - C291. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
J. P. Giblin, J. L. Leaney, and A. Tinker The Molecular Assembly of ATP-sensitive Potassium Channels. DETERMINANTS ON THE PORE FORMING SUBUNIT J. Biol. Chem., August 6, 1999; 274(32): 22652 - 22659. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 M. Yamada, A. Inanobe, and Y. Kurachi G Protein Regulation of Potassium Ion Channels Pharmacol. Rev., December 1, 1998; 50(4): 723 - 757. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
R. C. Schuurink, S. F. Shartzer, A. Fath, and R. L. Jones Characterization of a calmodulin-binding transporter from the plasma membrane of barley aleurone PNAS, February 17, 1998; 95(4): 1944 - 1949. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
A. Collins, H.-h. Chuang, Y. N. Jan, and L. Y. Jan Scanning mutagenesis of the putative transmembrane segments of Kir2.1, an inward rectifier potassium channel PNAS, May 13, 1997; 94(10): 5456 - 5460. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
M. K. Lancaster, K. M. Dibb, C. C. Quinn, R. Leach, J.-K. Lee, J. B. C. Findlay, and M. R. Boyett Residues and Mechanisms for Slow Activation and Ba2+ Block of the Cardiac Muscarinic K+ Channel, Kir3.1/Kir3.4 J. Biol. Chem., November 10, 2000; 275(46): 35831 - 35839. [Abstract] [Full Text] [PDF]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
