کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
2067388 | 1077896 | 2008 | 11 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Alternatively spliced forms of the P180 ribosome receptor differ in their ability to induce the proliferation of rough endoplasmic reticulum
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موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
بیوفیزیک
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چکیده انگلیسی
Expression of the canine 180-kDa ribosome receptor p180 in yeast induces the synthesis of RER, and increases the mRNAs of secretory pathway proteins, and protein secretion. To assess whether p180 is a master regulator of cell secretion in mammalian cells, we stably expressed red fluorescent forms of the human p180 variants p180ÎR (no tandem repeats), p180R (26 repeats), and full-length p180FR (54 repeats) containing different lengths of the tandem repeat ribosome-binding domain in rat pancreatic RINm5F islet β-cells. All three fluorescent p180 variants localized exclusively to the RER. Cells transfected with p180R were filled with ribosome-studded karmellae, whereas p180ÎR and p180FR transfectants contained only increased amounts of mostly smooth ER. Unlike in yeast, over-expression of p180R failed to increase the secretory pathway proteins calnexin, SEC61β, and calreticulin, or ribosome biogenesis. The data suggest that alternative splicing of the p180 tandem repeat domain is a means of regulating the ribosome-binding activity of p180, and potentially the secretory activity of the cell. However, p180 is not a master regulator of mammalian cell secretion as it does not concomitantly trigger the synthesis of protein machinery required to enhance protein synthesis and cell secretion.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Cell Biology International - Volume 32, Issue 5, May 2008, Pages 473-483
Journal: Cell Biology International - Volume 32, Issue 5, May 2008, Pages 473-483
نویسندگان
Ji-Zhong Bai, Euphemia Leung, Hilary Holloway, Geoffrey W. Krissansen,