کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10803088 | 1055772 | 2008 | 9 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Identification of a functional interaction between Kv4.3 channels and c-Src tyrosine kinase
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کلمات کلیدی
GSTPAGEKv4.3SH2 and SH3c-Srcvoltage-dependent K+polyacrylamide gel electrophoresis - الکتروفورز ژل پلی آکریل آمیدProtein-protein interactions - تعاملات پروتئین-پروتئینPhosphorylation - فسفریلاسیونProtein tyrosine kinases - پروتئین تیروزین کینازPotassium channels - کانال های پتاسیمglutathione S-transferase - گلوتاتیون S-ترانسفراز
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Identification of a functional interaction between Kv4.3 channels and c-Src tyrosine kinase Identification of a functional interaction between Kv4.3 channels and c-Src tyrosine kinase](/preview/png/10803088.png)
چکیده انگلیسی
Voltage-gated K+ (Kv) channels are key determinants of cardiac and neuronal excitability. A substantial body of evidence has accumulated in support of a role for Src family tyrosine kinases in the regulation of Kv channels. In this study, we examined the possibility that c-Src tyrosine kinase participates in the modulation of the transient voltage-dependent K+ channel Kv4.3. Supporting a mechanistic link between Kv4.3 and c-Src, confocal microscopy analysis of HEK293 cells stably transfected with Kv4.3 showed high degree of co-localization of the two proteins at the plasma membrane. Our results further demonstrate an association between Kv4.3 and c-Src by co-immunoprecipitation and GST pull-down assays, this interaction being mediated by the SH2 and SH3 domains of c-Src. Furthermore, we show that Kv4.3 is tyrosine phosphorylated under basal conditions. The functional relevance of the observed interaction between Kv4.3 and c-Src was established in patch-clamp experiments, where application of the Src inhibitor PP2 caused a decrease in Kv4.3 peak current amplitude, but not the inactive structural analogue PP3. Conversely, intracellular application of recombinant c-Src kinase or the protein tyrosine phosphatase inhibitor bpV(phen) increased Kv4.3 peak current amplitude. In conclusion, our findings provide evidence that c-Src-induced Kv4.3 channel activation involves their association in a macromolecular complex and suggest a role for c-Src-Kv4.3 pathway in regulating cardiac and neuronal excitability.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochimica et Biophysica Acta (BBA) - Molecular Cell Research - Volume 1783, Issue 10, October 2008, Pages 1884-1892
Journal: Biochimica et Biophysica Acta (BBA) - Molecular Cell Research - Volume 1783, Issue 10, October 2008, Pages 1884-1892
نویسندگان
Pedro Gomes, Tomoaki Saito, Cris del Corsso, Abderrahmane Alioua, Mansoureh Eghbali, Ligia Toro, Enrico Stefani,