@article{111206,
  keywords = {Humans, Tumor Cells, Cultured, Serine, Glyceric Acids, Phosphoglycerate Mutase},
  author = {Rob Oslund and Xiaoyang Su and Michael Haugbro and Jung-Min Kee and Mark Esposito and Yael David and Boyuan Wang and Eva Ge and David Perlman and Yibin Kang and Tom Muir and Joshua Rabinowitz},
  title = {Bisphosphoglycerate mutase controls serine pathway flux via 3-phosphoglycerate},
  abstract = {<p>Lower glycolysis involves a series of reversible reactions, which interconvert intermediates that also feed anabolic pathways. 3-phosphoglycerate (3-PG) is an abundant lower glycolytic intermediate that feeds serine biosynthesis via the enzyme phosphoglycerate dehydrogenase, which is genomically amplified in several cancers. Phosphoglycerate mutase 1 (PGAM1) catalyzes the isomerization of 3-PG into the downstream glycolytic intermediate 2-phosphoglycerate (2-PG). PGAM1 needs to be histidine phosphorylated to become catalytically active. We show that the primary PGAM1 histidine phosphate donor is 2,3-bisphosphoglycerate (2,3-BPG), which is made from the glycolytic intermediate 1,3-bisphosphoglycerate (1,3-BPG) by bisphosphoglycerate mutase (BPGM). When BPGM is knocked out, 1,3-BPG can directly phosphorylate PGAM1. In this case, PGAM1 phosphorylation and activity are decreased, but nevertheless sufficient to maintain normal glycolytic flux and cellular growth rate. 3-PG, however, accumulates, leading to increased serine synthesis. Thus, one biological function of BPGM is controlling glycolytic intermediate levels and thereby serine biosynthetic flux.</p>
},
  year = {2017},
  journal = {Nat Chem Biol},
  volume = {13},
  pages = {1081-1087},
  month = {10/2017},
  issn = {1552-4469},
  doi = {10.1038/nchembio.2453},
  language = {eng},
}