کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10815449 | 1058475 | 2013 | 8 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Modification of p115RhoGEF Ser330 regulates its RhoGEF activity
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کلمات کلیدی
DMEMLPAPDZphorbol 12-myristate 13-acetateS1PSpodoptera frugiperdaRhoASf9PAR-1TPCKTLCKFBSatRA - ATRAGTPase Activating Protein - GTPase فعال کردن پروتئینHPLC–MS/MS - HPLC-MS / MSLC/MS/MS - LC / MS / MSPMA - LDC هاDulbecco's modified Eagle's medium - Medal of Eagle اصلاح شده Dulbeccoall-trans retinoic acid - آل – ترانس رتینوئیک اسیدSphingosine-1-phosphate - اسپینگسین-1-فسفاتlysophosphatidic acid - اسید لیسفسفیدیدSurface plasmon resonance - تشدید پلاسمون سطحیSPR - تشدید پلاسمون سطحیlarg - دورfetal bovine serum - سرم جنین گاوGAP - شکافSignal transduction - هدایت سیگنالDbl homology - همبستگی DblPleckstrin Homology - همخوانی Pleckstrinresponse units - واحدهای پاسخLiquid chromatography/tandem mass spectrometry - کروماتوگرافی مایع / طیف سنج جرم دو طرفهProtease-activated receptor 1 - گیرنده پروتئاز فعال شده 1
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
p115RhoGEF is a member of a family of Rho-specific guanine nucleotide exchange factors that also contains a regulator of G protein signaling homology domain (RH-RhoGEFs) that serves as a link between Gα13 signaling and RhoA activation. While the mechanism of regulation of p115RhoGEF by Gα13 is becoming well-known, the role of other regulatory mechanisms, such as post-translational modification or autoinhibition, in mediating p115RhoGEF activity is less well-characterized. Here, putative phosphorylation sites on p115RhoGEF are identified and characterized. Mutation of Ser330 leads to a decrease in serum response element-mediated transcription as well as decreased activation by Gα13 in vitro. Additionally, this study provides the first report of the binding kinetics between full-length p115RhoGEF and RhoA in its various nucleotide states and examines the binding kinetics of phospho-mutant p115RhoGEF to RhoA. These data, together with other recent reports on regulatory mechanisms of p115RhoGEF, suggest that this putative phosphorylation site serves as a means for initiation or relief of autoinhibition of p115RhoGEF, providing further insight into the regulation of its activity.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Cellular Signalling - Volume 25, Issue 11, November 2013, Pages 2085-2092
Journal: Cellular Signalling - Volume 25, Issue 11, November 2013, Pages 2085-2092
نویسندگان
Christina R. Chow, Nobuchika Suzuki, Takeshi Kawamura, Takao Hamakubo, Tohru Kozasa,