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          Institute: MPI für medizinische Forschung     Collection: Abteilung Zellphysiologie     Display Documents



ID: 22444.0, MPI für medizinische Forschung / Abteilung Zellphysiologie
Kir2.1 inward rectifier K+ channels are regulated independently by protein kinases and ATP hydrolysis
Translation of Title:Kir2.1 inward rectifier K<SUP>+</SUP> channels are regulated independently by protein kinases and ATP hydrolysis
Authors:Fakler, Bernd; Brändle, Uwe; Glowatzki, E.; Zenner, H. P.; Ruppersberg, J. Peter
Language:English
Date of Publication (YYYY-MM-DD):1994-12
Title of Journal:Neuron
Journal Abbrev.:Neuron
Volume:13
Issue / Number:6
Start Page:1413
End Page:1420
Review Status:Peer-review
Audience:Experts Only
Intended Educational Use:No
Abstract / Description: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 microM free Mg2+ to the cytoplasmic side of the patch. As restoration could not be induced by the ATP analogs AMP-PNP or ATP gamma S, 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.
External Publication Status:published
Document Type:Article
Communicated by:Wulf Kaiser
Affiliations:MPI für medizinische Forschung/Abteilung Zellphysiologie/
Identifiers:URI:http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=... [Abstract]
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