کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10905376 | 1086751 | 2005 | 10 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Tyrosine-phosphorylated Hic-5 inhibits epidermal growth factor-induced lamellipodia formation
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کلمات کلیدی
p21 binding domainCSKPBDRho GTPasesARA55ECMPDGFPaxillinPBS2EGFCell motility - تحرک سلولیEMT - تکنسین فوریتهای پزشکیSH2 domain - دامنه SH2Hic-5 - در اینجا 5actin cytoskeleton - سی تی اسکن آکتینepidermal growth factor - عامل رشد اپیدرمیplatelet-derived growth factor - فاکتور رشد حاصل از پلاکتPervanadate - فرانسویExtracellular matrix - ماتریکس خارج سلولیAdhesion - چسبندگیEpithelial–mesenchymal transition - گذار اپیتلیال-مزانشیمی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
تحقیقات سرطان
پیش نمایش صفحه اول مقاله

چکیده انگلیسی
The focal adhesion protein Hic-5, a homologue to paxillin, has been shown to be tyrosine-phosphorylated in fibroblasts in response to stimuli such as osmotic stress, serum, LPA and endothelin. However, the function of this modification to Hic-5 is unclear. Herein, we show that Hic-5 is tyrosine-phosphorylated on residues 38 and 60 following epidermal growth factor (EGF) treatment of COS-7 cells, coincident with an increase in peripheral actin reorganization. To explore the role of Hic-5 phosphorylation in this process, we introduced wild-type (WT) and mutant Hic-5 constructs into COS-7 cells and determined that EGF-induced lamellipodia formation was suppressed by WT Hic-5. This effect required localization to focal adhesions as well as phosphorylation of Hic-5 as overexpression of both a non-targeting and a non-phosphorylatable Hic-5 failed to inhibit peripheral actin reorganization. Interestingly, overexpression of non-phosphorylatable Y31/118F or WT paxillin did not affect lamellipodia formation, indicating that this effect is specific to Hic-5. The EGF-induced lamellipodia were Rac-dependent and overexpressed WT Hic-5, but not non-phosphorylatable Hic-5 inhibited Rac activation. Our data suggest that Hic-5 tyrosine phosphorylation functions to regulate signaling associated with lamellipodia formation, a process fundamental to cell motility.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Experimental Cell Research - Volume 311, Issue 1, 15 November 2005, Pages 147-156
Journal: Experimental Cell Research - Volume 311, Issue 1, 15 November 2005, Pages 147-156
نویسندگان
Sara E. Hetey, David P. LaLonde, Christopher E. Turner,