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  Kir2.1 inward rectifier K+ channels are regulated independently by protein kinases and ATP hydrolysis

Fakler, B., Brändle, U., Glowatzki, E., Zenner, H., & Ruppersberg, J. P. (1994). Kir2.1 inward rectifier K+ channels are regulated independently by protein kinases and ATP hydrolysis. Neuron, 13(6), 1413-1420. doi:10.1016/0896-6273(94)90426-X.

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Fakler, Bernd, Author
Brändle, Uwe, Author
Glowatzki, Elisabeth, Author
Zenner, Hans−Peter, Author
Ruppersberg, J. Peter1, Author           
Affiliations:
1Department of Cell Physiology, Max Planck Institute for Medical Research, Max Planck Society, ou_1497701              

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 Abstract: Second messenger regulation of IRK1 (Kir2.1) inward rectifier K+ channels was investigated in giant inside-out patches from Xenopus oocytes. Kir2.1-mediated currents that run down completely within minutes upon excision of the patches could be partly restored by application of Mg-ATP together with <10 M free Mg2+ to the cytoplasmic side of the patch. As restoration could not be induced by the ATP analogs AMP-PNP or ATPS, this suggests an ATPase-like mechanism. In addition to ATP, the catalytic subunit of cAMP-dependent protein kinase (PKA) induced an increase in current amplitude, which could, however, only be observed if channels were previously or subsequently stimulated by Mg-ATP and free Mg2+. This indicates that functional activity of Kir2.1 channels requires both phosphorylation by PKA and ATP hydrolysis. Moreover, currents could be down-regulated by N-heptyl-5-chloro-1-naphthalenesulfonamide, a specific stimulator of protein kinase C (PKC), suggesting that PKA and PKC mediate inverse effects on Kir2.1 channels. Regulation of Kir2.1 channels described here may be an important mechanism for regulation of excitability.

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Language(s): eng - English
 Dates: 1994-06-071994-10-082004-04-221994-12-06
 Publication Status: Issued
 Pages: 8
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 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 666747
DOI: 10.1016/0896-6273(94)90426-X
Other: 4108
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Title: Neuron
Source Genre: Journal
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Publ. Info: Cambridge, Mass. : Cell Press
Pages: - Volume / Issue: 13 (6) Sequence Number: - Start / End Page: 1413 - 1420 Identifier: ISSN: 0896-6273
CoNE: https://pure.mpg.de/cone/journals/resource/954925560565