Editors' ChoiceBiochemistry

Metabolic Sensor

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Science Signaling  28 Aug 2012:
Vol. 5, Issue 239, pp. ec225
DOI: 10.1126/scisignal.2003530

The enzyme O-GlcNAc transferase (OGT) catalyzes the transfer of N-acetylglucosamine from uridine diphospho-N-acetylglucosamine (UDP-GlcNAc) to serine or threonine residues of intracellular proteins and responds to the metabolic status of the cell. Yi et al. (see the Perspective by Mattaini and Vander Heiden) show that O-GlcNAcylation of phosphofructokinase 1 (PFK1) reduces its activity, thus influencing rates of glycolysis within cells. O-GlcNAcylation of PFK1 was increased in cells exposed to hypoxia and was increased in several cell lines derived from human tumors. Thus, metabolic changes mediated by O-GlcNAcylation may benefit anabolism and growth of cancer cells. However, glycosylation of PFK1 was not detected in rapidly proliferating normal cells.

W. Yi, P. M. Clark, D. E. Mason, M. C. Keenan, C. Hill, W. A. Goddard III, E. C. Peters, E. M. Driggers, L. C. Hsieh-Wilson, Phosphofructokinase 1 glycosylation regulates cell growth and metabolism. Science 337, 975–980 (2012). [Abstract] [Full Text]

K. R. Mattaini, M. G. Vander Heiden, Glycosylation to adapt to stress. Science 337, 925–926 (2012). [Abstract] [Full Text]

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