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• W2017507172 abstract "Recent studies have implicated Epac2, a guanine-nucleotide exchange factor for the Rap subfamily of monomeric G proteins, as an important regulator of insulin secretion from pancreatic β-cells. Although the Epac proteins were originally identified as cAMP-responsive activators of Rap1 GTPases, the role of Rap1 in β-cell biology has not yet been defined. In this study, we examined the direct effects of Rap1 signaling on β-cell biology. Using the Ins-1 rat insulinoma line, we demonstrate that activated Rap1A, but not related monomeric G proteins, promotes ribosomal protein S6 phosphorylation. Using isolated rat islets, we show that this signaling event is rapamycin-sensitive, indicating that it is mediated by the mammalian target of rapamycin complex 1-p70 S6 kinase pathway, a known growth regulatory pathway. This newly defined β-cell signaling pathway acts downstream of cAMP, in parallel with the stimulation of cAMP-dependent protein kinase, to drive ribosomal protein S6 phosphorylation. Activated Rap1A promotes glucose-stimulated insulin secretion, islet cell hypertrophy, and islet cell proliferation, the latter exclusively through mammalian target of rapamycin complex 1, suggesting that Rap1 is an important regulator of β-cell function. This newly defined signaling pathway may yield unique targets for the treatment of β-cell dysfunction in diabetes." @default.
• W2017507172 created "2016-06-24" @default.
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• W2017507172 date "2010-05-01" @default.
• W2017507172 modified "2023-10-16" @default.
• W2017507172 title "Rap1 Promotes Multiple Pancreatic Islet Cell Functions and Signals through Mammalian Target of Rapamycin Complex 1 to Enhance Proliferation" @default.
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• W2017507172 doi "https://doi.org/10.1074/jbc.m109.069112" @default.
• W2017507172 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2871445" @default.
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