{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,28]],"date-time":"2026-09-28T16:12:05Z","timestamp":1790611925767,"version":"4.1.0"},"reference-count":14,"publisher":"Portland Press Ltd.","issue":"7","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2017,4,1]]},"abstract":"<jats:p>Maintaining a steady balance between nutrient supply and energy demand is essential for all living organisms and is achieved through the dynamic control of metabolic processes that produce and consume adenosine-5\u2032-triphosphate (ATP), the universal currency of energy in all cells. A key sensor of cellular energy is the adenosine-5\u2032-monophosphate (AMP)-activated protein kinase (AMPK), which is the core component of a signaling network that regulates energy and nutrient metabolism. AMPK is activated by metabolic stresses that decrease cellular ATP, and functions to restore energy balance by orchestrating a switch in metabolism away from anabolic pathways toward energy-generating catabolic processes. A new study published in a recent issue of Biochemical Journal by Zibrova et al. shows that glutamine:fructose-6-phosphate amidotransferase-1 (GFAT1), the rate-limiting enzyme of the hexosamine biosynthesis pathway (HBP), is a physiological substrate of AMPK. The HBP is an offshoot of the glycolytic pathway that drives the synthesis of uridine-5\u2032-diphospho-N-acetylglucosamine, the requisite donor metabolite needed for dynamic \u03b2-N-acetylglucosamine (O-GlcNAc) modification (O-GlcNAcylation) of cellular proteins. O-GlcNAcylation is a nutrient-sensitive post-translational modification that, like phosphorylation, regulates numerous intracellular processes. Zibrova et al. show that inhibitory phosphorylation of the GFAT1 residue Ser243 by AMPK in response to physiological or small-molecule activators leads to a reduction in cellular protein O-GlcNAcylation. Further work revealed that AMPK-dependent phosphorylation of GFAT1 promotes angiogenesis in endothelial cells. This elegant study demonstrates that the AMPK\u2013GFAT1 signaling axis serves as an important communication point between two nutrient-sensitive signaling pathways and is likely to play a significant role in controlling physiological processes in many other tissues.<\/jats:p>","DOI":"10.1042\/bcj20170006","type":"journal-article","created":{"date-parts":[[2017,3,24]],"date-time":"2017-03-24T00:33:37Z","timestamp":1490315617000},"page":"1289-1292","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":21,"title":["The sweet side of AMPK signaling: regulation of GFAT1"],"prefix":"10.1042","volume":"474","author":[{"given":"John W.","family":"Scott","sequence":"first","affiliation":[{"name":"St Vincent's Institute and Department of Medicine, University of Melbourne, 41 Victoria Parade, Fitzroy 3065, Australia"},{"name":"Mary MacKillop Institute for Health Research, Australian Catholic University, 215 Spring Street, Melbourne 3000, Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jonathan S.","family":"Oakhill","sequence":"additional","affiliation":[{"name":"St Vincent's Institute and Department of Medicine, University of Melbourne, 41 Victoria Parade, Fitzroy 3065, Australia"},{"name":"Mary MacKillop Institute for Health Research, Australian Catholic University, 215 Spring Street, Melbourne 3000, Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"288","published-online":{"date-parts":[[2017,3,23]]},"reference":[{"key":"2021112216511494300_BCJ-2017-0006CC1","doi-asserted-by":"publisher","first-page":"2987","DOI":"10.1111\/febs.13698","article-title":"AMP-activated protein kinase: a cellular energy sensor that comes in 12 flavours","volume":"283","author":"Ross","year":"2016","journal-title":"FEBS J."},{"key":"2021112216511494300_BCJ-2017-0006CC2","doi-asserted-by":"publisher","first-page":"983","DOI":"10.1042\/BCJ20160980","article-title":"GFAT1 phosphorylation by AMPK promotes VEGF-induced angiogenesis","volume":"474","author":"Zibrova","year":"2017","journal-title":"Biochem. 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