Phosphofructokinase 1 glycosylation regulates cell growth and metabolism
| Autor: | William A. Goddard, Linda C. Hsieh-Wilson, Peter M. Clark, Collin Hill, Marie C. Keenan, Edward M. Driggers, Wen Yi, Eric C. Peters, Daniel E. Mason |
|---|---|
| Rok vydání: | 2012 |
| Předmět: |
Glycosylation
Acylation Mice Nude Biology Pentose phosphate pathway N-Acetylglucosaminyltransferases Acetylglucosamine Cell Line Serine Pentose Phosphate Pathway chemistry.chemical_compound Mice Adenosine Triphosphate Cell Line Tumor Neoplasms Animals Humans Glycolysis Lactic Acid Phosphofructokinase-1 Liver Type Cell Proliferation Multidisciplinary Cell growth Metabolism Cell Hypoxia Metabolic pathway Glucose Biochemistry chemistry Cancer cell NADP |
| Zdroj: | Science (New York, N.Y.). 337(6097) |
| ISSN: | 1095-9203 |
| Popis: | Metabolic Sensor 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. (p. 975 ; 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. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|