کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
8322733 | 1539882 | 2015 | 10 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Tomosyn is a novel Akt substrate mediating insulin-dependent GLUT4 exocytosis
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کلمات کلیدی
SUMOeGFPGSTpKaVAMPSNAREGLUT4SNAP-25Akt - آکتsmall ubiquitin-related modifier - اصلاح کننده کوچک کوچک ubiquitinsodium dodecyl sulfate-polyacrylamide gel electrophoresis - الکتروفورز ژل دوده سولفات سدیم پلی آکریل آمیدSDS-PAGE - الکتروفورز ژل پلی آکریل آمیدExocytosis - اگزوسیتوزglucose transporter 4 - حمل کننده گلوکز 4Phosphorylation - فسفریلاسیونwild type - نوع وحشیVesicle-associated membrane protein - پروتئین غشاء مرتبط با Vesicleenhanced green fluorescence protein - پروتئین فلورسانس سبز افزایش یافته استsynaptosome-associated protein of 25 kDa - پروتئین مرتبط با سیناپتوزوم 25 کیلو دالتونprotein kinase A - پروتئین کیناز Aglutathione 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: Tomosyn is a novel Akt substrate mediating insulin-dependent GLUT4 exocytosis Tomosyn is a novel Akt substrate mediating insulin-dependent GLUT4 exocytosis](/preview/png/8322733.png)
چکیده انگلیسی
Insulin triggers glucose uptake into skeletal muscle and adipose tissues by gaining the available number of glucose transporter 4 (GLUT4) on the cell surface. GLUT4-loaded vesicles are targeted to plasma membrane from the intracellular reservoir through multiple trafficking and fusion processes that are mainly regulated by Akt. However, it is still largely unknown how GLUT4 expression in the cell surface is promoted by insulin. In the present study, we identified tomosyn at Ser-783 as a possible Akt-substrate motif and examined whether the phosphorylation at Ser-783 is involved in the regulation of GLUT4 expression. Both Akt1 and Akt2 phosphorylated the wild-type tomosyn, but not the mutant tomosyn in which Ser-783 was replaced with Ala. Phosphorylation of tomosyn at Ser-783 was also observed in the intact cells by insulin stimulation, which was blocked by PI3K inhibitor, LY294002. In vitro pull-down assay showed that phosphorylation of tomosyn at Ser-783 by Akt inhibited the interaction with syntaxin 4. Insulin stimulation increased GLUT4 in the cell surface of CHO-K1 cells to promote glucose uptake, however exogenous expression of the mutant tomosyn attenuated the increase by insulin. These results suggest that Ser-783 of tomosyn is a target of Akt and is implicated in the interaction with syntaxin 4.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: The International Journal of Biochemistry & Cell Biology - Volume 62, May 2015, Pages 62-71
Journal: The International Journal of Biochemistry & Cell Biology - Volume 62, May 2015, Pages 62-71
نویسندگان
Koki Nagano, Hiroshi Takeuchi, Jing Gao, Yoshihide Mori, Takahito Otani, DaGuang Wang, Masato Hirata,