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Science 6 November 1998:
Vol. 282. no. 5391, pp. 1138 - 1141
DOI: 10.1126/science.282.5391.1138
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Reports

Membrane Phospholipid Control of Nucleotide Sensitivity of KATP Channels

S.-L. Shyng, C. G. Nichols *

Adenosine triphosphate (ATP)-sensitive potassium (KATP) channels couple cell metabolism to electrical activity. Phosphatidylinositol phosphates (PIPs) profoundly antagonized ATP inhibition of KATP channels when applied to inside-out membrane patches. It is proposed that membrane-incorporated PIPs can bind to positive charges in the cytoplasmic region of the channel's Kir6.2 subunit, stabilizing the open state of the channel and antagonizing the inhibitory effect of ATP. The tremendous effect of PIPs on ATP sensitivity suggests that in vivo alterations of membrane PIP levels will have substantial effects on KATP channel activity and hence on the gain of metabolism-excitation coupling.

Department of Cell Biology and Physiology, Washington University School of Medicine, 660 South Euclid Avenue, St. Louis, MO 63110, USA.
*   To whom correspondence should be addressed. E-mail: cnichols{at}cellbio.wustl.edu

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Coupling of Cell Energetics with Membrane Metabolic Sensing. INTEGRATIVE SIGNALING THROUGH CREATINE KINASE PHOSPHOTRANSFER DISRUPTED BY M-CK GENE KNOCK-OUT.
M. R. Abraham, V. A. Selivanov, D. M. Hodgson, D. Pucar, L. V. Zingman, B. Wieringa, P. P. Dzeja, A. E. Alekseev, and A. Terzic (2002)
J. Biol. Chem. 277, 24427-24434
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The Carboxyl Termini of KATP Channels Bind Nucleotides.
C. G. Vanoye, G. G. MacGregor, K. Dong, L. Tang, A. S. Buschmann, A. E. Hall, M. Lu, G. Giebisch, and S. C. Hebert (2002)
J. Biol. Chem. 277, 23260-23270
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Structural and Functional Determinants of Conserved Lipid Interaction Domains of Inward Rectifying Kir6.2 Channels.
C. A. Cukras, I. Jeliazkova, and C. G. Nichols (2002)
J. Gen. Physiol. 119, 581-591
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Protein kinase C modulation of recombinant ATP-sensitive K+ channels composed of Kir6.1 and/or Kir6.2 expressed with SUR2B.
K. S Thorneloe, Y. Maruyama, A T. Malcolm, P. E Light, M. P Walsh, and W. C Cole (2002)
J. Physiol. 541, 65-80
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Histamine promotes excitability in bovine adrenal chromaffin cells by inhibiting an M-current.
D. J Wallace, C. Chen, and P. D Marley (2002)
J. Physiol. 540, 921-939
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