Please note that eDoc will be permanently shut down in the first quarter of 2021!      Home News About Us Contact Contributors Disclaimer Privacy Policy Help FAQ

Quick Search
My eDoc
Session History
Support Wiki
Direct access to
document ID:

          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
Date of Publication (YYYY-MM-DD):1994-12
Title of Journal:Neuron
Journal Abbrev.:Neuron
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: [Abstract]
The scope and number of records on eDoc is subject to the collection policies defined by each institute - see "info" button in the collection browse view.