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Yi, Wen; Clark, Peter M.; Mason, Daniel E.; Keenan, Marie C.; Hill, Collin; Goddard, William A.; Peters, Eric C.; Driggers, Edward M.; Hsieh-Wilson, Linda C.
Science (American Association for the Advancement of Science), 08/2012, Letnik: 337, Številka: 6097Journal Article
Cancer cells must satisfy the metabolic demands of rapid cell growth within a continually changing microenvironment. We demonstrated that the dynamic posttranslational modification of proteins by O-linked β-N-acetylglucosamine (O-GlcNAcylation) is a key metabolic regulator of glucose metabolism. O-GlcNAcylation was induced at serine 529 of phosphofructokinase 1 (PFK1) in response to hypoxia. Glycosylation inhibited PFK1 activity and redirected glucose flux through the pentose phosphate pathway, thereby conferring a selective growth advantage on cancer cells. Blocking glycosylation of PFK1 at serine 529 reduced cancer cell proliferation in vitro and impaired tumor formation in vivo. These studies reveal a previously uncharacterized mechanism for the regulation of metabolic pathways in cancer and a possible target for therapeutic intervention.
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