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Conference Paper: Epidermal Growth Factor Receptor Tyrosine Kinase Stimulates Human Inward Rectifier Potassium (Kir2.3) Channels

TitleEpidermal Growth Factor Receptor Tyrosine Kinase Stimulates Human Inward Rectifier Potassium (Kir2.3) Channels
Authors
Issue Date2009
PublisherCell Press
Citation
53th Annual Meeting of Biophysical Society, Boston, MA. In Biophysical Journal, 2009, v. 96 n. 3 S1, p. 462a–463a How to Cite?
AbstractProtein tyrosine kinases (PTKs), in addition to the mediation of cellular events such as cell growth, differentiation, etc., regulate ion channels. Although Kir2.3 channel plays a crucial role in the repolarization and membrane potential stabilization of neurons and myocardium, modulation of this channel is not fully understood. The present study investigated whether/how human Kir2.3 channel is modulated by PTKs and protein tyrosine phosphatases (PTPs) in HEK 239 cells stably expressing Kir2.3 gene using approaches of whole-cell patch voltage clamp, immunoprecipitation and Western blot, and site-directed mutagenesis. We found that epidermal growth factor (EGF, 100 ng/ml) and PTPs inhibitor orthovanadate (1 mM) significantly enhanced Kir2.3 channel current, while the broad spectrum PTKs inhibitor genistein and the selective EGF receptor kinase inhibitor AG556, but not the Src-family PTK inhibitor PP2 or the platelet-derived growth factor receptor kinase inhibitor AG1295, suppressed the current. The inhibitory effect of Kir2.3 current by genistein or AG556 was fully countered by EGF or orthovanadate. In addition, tyrosine phosphorylation level of Kir2.3 channel was increased by EGF or orthovanadate, but decreased by genistein or AG556. The reduced phosphorylation level by genistein or AG556 was reversed by EGF or orthovanadate. Interestingly, the response of Kir2.3 channel to EGF or AG556 disappeared in Kir2.3 Y234A mutant. Our results demonstrate the novel information that human Kir2.3 channel is stimulated by EGFR tyrosine kinase via phosphorylating the channel at Tyr234.
Persistent Identifierhttp://hdl.handle.net/10722/62449
ISSN
2015 Impact Factor: 3.632
2015 SCImago Journal Rankings: 2.188

 

DC FieldValueLanguage
dc.contributor.authorZhang, Den_HK
dc.contributor.authorLau, CPen_HK
dc.contributor.authorLi, GRen_HK
dc.date.accessioned2010-07-13T04:01:27Z-
dc.date.available2010-07-13T04:01:27Z-
dc.date.issued2009en_HK
dc.identifier.citation53th Annual Meeting of Biophysical Society, Boston, MA. In Biophysical Journal, 2009, v. 96 n. 3 S1, p. 462a–463aen_HK
dc.identifier.issn0006-3495-
dc.identifier.urihttp://hdl.handle.net/10722/62449-
dc.description.abstractProtein tyrosine kinases (PTKs), in addition to the mediation of cellular events such as cell growth, differentiation, etc., regulate ion channels. Although Kir2.3 channel plays a crucial role in the repolarization and membrane potential stabilization of neurons and myocardium, modulation of this channel is not fully understood. The present study investigated whether/how human Kir2.3 channel is modulated by PTKs and protein tyrosine phosphatases (PTPs) in HEK 239 cells stably expressing Kir2.3 gene using approaches of whole-cell patch voltage clamp, immunoprecipitation and Western blot, and site-directed mutagenesis. We found that epidermal growth factor (EGF, 100 ng/ml) and PTPs inhibitor orthovanadate (1 mM) significantly enhanced Kir2.3 channel current, while the broad spectrum PTKs inhibitor genistein and the selective EGF receptor kinase inhibitor AG556, but not the Src-family PTK inhibitor PP2 or the platelet-derived growth factor receptor kinase inhibitor AG1295, suppressed the current. The inhibitory effect of Kir2.3 current by genistein or AG556 was fully countered by EGF or orthovanadate. In addition, tyrosine phosphorylation level of Kir2.3 channel was increased by EGF or orthovanadate, but decreased by genistein or AG556. The reduced phosphorylation level by genistein or AG556 was reversed by EGF or orthovanadate. Interestingly, the response of Kir2.3 channel to EGF or AG556 disappeared in Kir2.3 Y234A mutant. Our results demonstrate the novel information that human Kir2.3 channel is stimulated by EGFR tyrosine kinase via phosphorylating the channel at Tyr234.-
dc.languageengen_HK
dc.publisherCell Press-
dc.relation.ispartofBiophysical Journal-
dc.titleEpidermal Growth Factor Receptor Tyrosine Kinase Stimulates Human Inward Rectifier Potassium (Kir2.3) Channelsen_HK
dc.typeConference_Paperen_HK
dc.identifier.emailLau, CP: cplau@hku.hken_HK
dc.identifier.emailLi, GR: grli@hkucc.hku.hken_HK
dc.identifier.authorityLi, GR=rp00476en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1016/j.bpj.2008.12.2382-
dc.identifier.hkuros155212en_HK

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