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© Giulia Manina, Institut Pasteur
Mycobacterium tuberculosis dual fluorescent reporter of metabolic activity. Green (active bacilli) and red fluorescence (quiescent bacilli) are merged, 100X magnification.
Publication : FEBS letters

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

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in FEBS letters - 05 Mar 2008

Kuo M, Zilberfarb V, Gangneux N, Christeff N, Issad T,

Link to Pubmed [PMID] – 18280254

Link to DOI – 10.1016/j.febslet.2008.02.010

FEBS Lett 2008 Mar; 582(5): 829-34

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.

https://pubmed.ncbi.nlm.nih.gov/18280254