Abstract
In this issue of Cell Metabolism, Daniel Drucker and colleagues (Yusta et al., 2006) explore how the incretin mimetic exendin-4 improves beta cell function and survival during ER stress. Their findings suggest that protein kinase A signaling elicited by GLP-1 receptor activation differentially modulates one arm of the unfolded protein response (UPR). Regulation of this UPR pathway leads to enhanced translational expression of ATF4, a transcription factor central for stress remedy and cell survival.
MeSH terms
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Activating Transcription Factor 4 / genetics
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Activating Transcription Factor 4 / metabolism*
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Animals
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Cell Survival
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Exenatide
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Glucagon-Like Peptide-1 Receptor
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Hypoglycemic Agents / pharmacology
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Insulin-Secreting Cells / drug effects
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Insulin-Secreting Cells / physiology*
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Mice
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Peptides / pharmacology
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Peptides / physiology*
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Protein Biosynthesis*
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Protein Folding
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Receptors, Glucagon / metabolism*
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Receptors, Glucagon / physiology
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Up-Regulation / drug effects
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Venoms / pharmacology
Substances
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ATF4 protein, human
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GLP1R protein, human
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Glp1r protein, mouse
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Glucagon-Like Peptide-1 Receptor
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Hypoglycemic Agents
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Peptides
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Receptors, Glucagon
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Venoms
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Activating Transcription Factor 4
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Exenatide