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Titolo:
Acute suppression of inwardly rectifying Kir2.1 channels by direct tyrosine kinase phosphorylation
Autore:
Wischmeyer, E; Doring, F; Karschin, A;
Indirizzi:
MaxGottingen,st Biophys Chem, Dept Mol Neurobiol Signal Transduct, D-37070Max Planck Inst Biophys Chem Gottingen Germany D-37070 ransduct, D-37070
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 51, volume: 273, anno: 1998,
pagine: 34063 - 34068
SICI:
0021-9258(199812)273:51<34063:ASOIRK>2.0.ZU;2-C
Fonte:
ISI
Lingua:
ENG
Soggetto:
KV1.3 POTASSIUM CHANNEL; GROWTH-FACTOR RECEPTOR; K+ CHANNEL; PROTEIN-PHOSPHORYLATION; NEUROTROPHIN RECEPTORS; DEPENDENT SUPPRESSION; INSULIN-RECEPTOR; ION CHANNELS; MODULATION; ACTIVATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
42
Recensione:
Indirizzi per estratti:
Indirizzo: Karschin, A Max Planck Inst Biophys Chem, Dept Mol Neurobiol Signal Transduct, Fassberg Max Planck Inst Biophys Chem Fassberg 11 Gottingen Germany D-37070
Citazione:
E. Wischmeyer et al., "Acute suppression of inwardly rectifying Kir2.1 channels by direct tyrosine kinase phosphorylation", J BIOL CHEM, 273(51), 1998, pp. 34063-34068

Abstract

Signaling via cytosolic and receptor tyrosine kinases is associated with cell growth and differentiation but also targets onto transmitter receptors and ion channels. Here, regulation by tyrosine kinase (TK) activity was investigated for inwardly rectifying K+ (Kir2.1) channels that control membrane excitability in many central neurons. In mammalian tsA-201 cells, the membrane-permeable protein tyrosine phosphatase inhibitor, perorthovanadate (100 mu M), suppressed currents through recombinant Kir2.1 channels by 60 +/-20%, Coapplication of the TK inhibitor genistein (100 mu M:) completely abolished this effect. Native Kir2.1 channels in rat basophilic leukocytes were affected by manipulation of the TK and protein tyrosine phosphatase activity in a qualitatively similar manner. Site mutation of a tyrosine consensus residue for TK phosphorylation in the C-terminal domain of Kir2.1 generated channel properties indistinguishable from wild-type Kir2.1 channels. However, Kir2.1Y242F channels were no longer suppressed following exposure toperorthovanadate, indicating that the channel is a direct substrate for TKs. After coexpression of nerve growth factor receptor with Kir2.1 channels in tsA-201 cells and Xenopus oocytes, the activity of Kir2.1 was rapidly suppressed by applied nerve growth factor (0.5 mu g/ml) by 31 +/- 10 and 21 +/- 15%, respectively, Acute inhibition was also evoked by epidermal growth factor and insulin via endogenous insulin receptors, indicating that Kir2.1channels may serve as a general target for neurotrophic growth factors in the brain.

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Documento generato il 24/10/20 alle ore 11:34:43