ArticleBritish journal of pharmacology2011
Epidermal growth factor receptor tyrosine kinase regulates the human inward rectifier potassium K(IR)2.3 channel, stably expressed in HEK 293 cells.
Article in British journal of pharmacology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 27 citations in OpenAlex.
- Elucidating the binding and metabolic interactions of sunitinib and sorafenib with Cytochrome P450s CYP2U1 and CYP2D6.Molecular pharmacology · 2026Article
- Tyrosine phosphorylation of Kir6.2 subunit negatively regulates cardiac KBasic research in cardiology · 2025Article
- Recurrent ventricular arrhythmias and heart failure induced by osimertinib- a case report.Frontiers in cardiovascular medicine · 2024Article
- Ion Channels as Potential Tools for the Diagnosis, Prognosis, and Treatment of HPV-Associated Cancers.Cells · 2023Review
- Case Report: Torsade de Pointes Induced by the Third-Generation Epidermal Growth Factor Receptor-Tyrosine Kinase Inhibitor Osimertinib Combined With Litsea Cubeba.Frontiers in cardiovascular medicine · 2022Article
- Genistein Directly Represses the Phosphorylation of STAT5 in Lactating Mammary Epithelial Cells.ACS omega · 2021Article
- Case Report: QT Prolongation and Abortive Sudden Death Observed in an 85-Year-Old Female Patient With Advanced Lung Cancer Treated With Tyrosine Kinase Inhibitor Osimertinib.Frontiers in cardiovascular medicine · 2021Article
- Effects of the Tumor Environment on Ion Channels: Implication for Breast Cancer Progression.Reviews of physiology, biochemistry and pharmacology · 2021Review
- Long noncoding RNA POU6F2-AS1 regulates lung cancer aggressiveness through sponging miR-34c-5p to modulate KCNJ4 expression.Genetics and molecular biology · 2021Article
- Article
- Cellular information dynamics through transmembrane flow of ions.Scientific reports · 2017Article
- Tyrphostin AG556 increases the activity of large conductance CaJournal of cellular and molecular medicine · 2017Article
- Genistein and tyrphostin AG556 decrease ultra-rapidly activating delayed rectifier KBritish journal of pharmacology · 2017Article
- Regulation of voltage-gated potassium channels attenuates resistance of side-population cells to gefitinib in the human lung cancer cell line NCI-H460.BMC pharmacology & toxicology · 2017Article
- Clinicopathologic Implications of Eukaryotic Initiation Factor 3f and Her-2/neu Expression in Gastric Cancer.Clinical and translational science · 2015Article
- The inward rectifier potassium channel Kir2.1 is expressed in mouse neutrophils from bone marrow and liver.American journal of physiology. Cell physiology · 2015Article
- Expression of Septin 2 and Her2/neu in Colorectal Cancer.Journal of microscopy and ultrastructureArticle
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
background and purposeThe detailed molecular modulation of inward rectifier potassium channels (including the K(IR) 2.3 channel) is not fully understood. The present study was designed to determine whether human K(IR) 2.3 (K(IR) 2.3) channels were regulated by protein tyrosine kinases (PTKs). EXPERIMENTAL APPROACH: Whole-cell patch voltage-clamp, immunoprecipitation, Western blot analysis and site-directed mutagenesis were employed to determine the potential PTK phosphorylation of Kir2.3 current in HEK 293 cells stably expressing Kir2.3 gene. KEY
resultsThe broad-spectrum PTK inhibitor genistein (10 µM) and the selective epidermal growth factor (EGF) kinase inhibitor AG556 (10 µM) reversibly decreased K(IR) 2.3 current and the effect was reversed by the protein tyrosine phosphatase inhibitor, orthovanadate (1 mM). Although EGF (100 ng·mL(-1) ) and orthovanadate enhanced K(IR) 2.3 current, this effect was antagonized by AG556. However, the Src-family tyrosine kinase inhibitor PP2 (10 µM) did not inhibit K(IR) 2.3 current. Tyrosine phosphorylation of K(IR) 2.3 channels was decreased by genistein or AG556, and was increased by EGF or orthovanadate. The decrease of tyrosine phosphorylation of K(IR) 2.3 channels by genistein or AG556 was reversed by orthovanadate or EGF. Interestingly, the response of K(IR) 2.3 channels to EGF or AG556 was lost in the K(IR) 2.3 Y234A mutant channel. CONCLUSION AND IMPLICATIONS: These results demonstrate that the EGF receptor tyrosine kinase up-regulates the K(IR) 2.3 channel via phosphorylation of the Y234 residue of the WT protein. This effect may be involved in the endogenous regulation of cellular electrical activity.
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