Moore, C.E.J., Xie, J., Gomez, E. and Herbert, T.P. (2009) Identification of cAMP-Dependent Kinase as a Third in Vivo Ribosomal Protein S6 Kinase in Pancreatic β-Cells. Journal of Molecular Biology, 389 (3). pp. 480-494. ISSN 0022-2836
Full content URL: https://www.sciencedirect.com/science/article/pii/...
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Item Type: | Article |
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Item Status: | Live Archive |
Abstract
Ribosomal protein S6 (rpS6) is phosphorylated in vivo by isoforms of p70 S6 protein kinase and p90 ribosomal S6 kinase, and there is good evidence that it plays a positive role in controlling pancreatic β-cell size and function. In this report, we demonstrate in the pancreatic β-cell line MIN6 (mouse insulinoma cell line 6) and islets of Langerhans that agents which stimulate increases in cAMP, such as glucagon-like peptide-1 and forskolin, lead to the phosphorylation of rpS6 at Ser235/Ser236 independently of the activation of the currently known in vivo rpS6 kinases via a pathway that is sensitive to inhibitors of cAMP-dependent protein kinase [protein kinase A (PKA)]. This cAMP-dependent rpS6 kinase activity is also sensitive to PKI in vitro, and PKA exclusively phosphorylates recombinant rpS6 on Ser235/Ser236 in vitro. With these data taken together, we conclude that PKA can phosphorylate rpS6 exclusively at Ser235/Ser236 in vivo in pancreatic β-cells, thus providing a potentially important link between cAMP signalling and the regulation of protein synthesis. Lastly, we provide evidence that PKA is also likely to phosphorylate rpS6 on Ser235/Ser236 in vivo in a number of other mammalian cell types.
Additional Information: | The final published version of this article can be accessed online at: https://www.sciencedirect.com/science/article/pii/S0022283609004501?via%3Dihub |
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Keywords: | rpS6, PKA, GLP1, S6Km, TORC1 |
Subjects: | A Medicine and Dentistry > A300 Clinical Medicine |
ID Code: | 28226 |
Deposited On: | 25 Jul 2018 11:44 |
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