期刊
SCIENCE
卷 341, 期 6145, 页码 549-553出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1238327
关键词
-
资金
- NIH [CA087660]
- Damon Runyon Cancer Research Foundation
- Skaggs Institute for Chemical Biology
The posttranslational modification of proteins and their regulation by metabolites represent conserved mechanisms in biology. At the confluence of these two processes, we report that the primary glycolytic intermediate 1,3-bisphosphoglycerate (1,3-BPG) reacts with select lysine residues in proteins to form 3-phosphoglyceryl-lysine (pgK). This reaction, which does not require enzyme catalysis, but rather exploits the electrophilicity of 1,3-BPG, was found by proteomic profiling to be enriched on diverse classes of proteins and prominently in or around the active sites of glycolytic enzymes. pgK modifications inhibit glycolytic enzymes and, in cells exposed to high glucose, accumulate on these enzymes to create a potential feedback mechanism that contributes to the buildup and redirection of glycolytic intermediates to alternate biosynthetic pathways.
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