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FEBS Lett. 2008 Mar 5;582(5):829-34. doi: 10.1016/j.febslet.2008.02.010. Epub 2008 Feb 14.

O-glycosylation of FoxO1 increases its transcriptional activity towards the glucose 6-phosphatase gene.

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  • 1Institut Cochin, Université Paris Descartes, 22 Rue Méchain, CNRS (UMR 8104), Paris, France.

Abstract

Mono-O-glycosylations post-translationally regulate the activity of nucleocytoplasmic proteins. We showed that glucosamine and an inhibitor of deglycosylation (PUGNAc) induced O-glycosylation of FoxO1, resulting in increased expression of a glucose-6-phosphatase reporter gene. This effect was independent of FoxO1 re-localisation, since it was also observed with constitutively nuclear FoxO1-AAA mutant. Moreover, in HepG2 cells, glucosamine and PUGNAc have a synergistic effect on the glucose-6-phosphatase reporter gene, and this effect was inhibited by FoxO1 siRNAs. Since glucose-6-phosphatase plays a key role in hepatic glucose production, our observation may be of importance with regard to glucotoxicity associated with chronic hyperglycaemia in diabetes.

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