Pyruvate kinase M2 is a phosphotyrosine-binding protein

Nature

Volumn 452, Issue 7184, 2008, Pages 181-186

  Christofk, Heather R ^a   Vander Heiden, Matthew G ^a,b   Wu, Ning ^a   Asara, John M ^a,c   Cantley, Lewis C ^a,c  

^a HARVARD MEDICAL SCHOOL   (United States)

^b DANA FARBER CANCER INSTITUTE   (United States)

^c BETH ISRAEL DEACONESS MEDICAL CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROTEIN; FRUCTOSE BISPHOSPHATASE; PEPTIDE; PHOSPHOTYROSINE; PYRUVATE KINASE; PYRUVATE KINASE M2; UNCLASSIFIED DRUG;

CANCER; CYTOLOGY; ENZYME ACTIVITY; METABOLITE; PROTEIN; SIGNALING;

ALLOSTERISM; ANIMAL CELL; ARTICLE; CELL GROWTH; CELL METABOLISM; CONTROLLED STUDY; ENERGY YIELD; ENZYME ACTIVITY; ENZYME BINDING; ENZYME INHIBITION; ENZYME MECHANISM; ENZYME REGULATION; GLUCOSE METABOLISM; GLYCOLYSIS; HUMAN; HUMAN CELL; METABOLITE; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN PHOSPHORYLATION; PROTEOMICS; SIGNAL TRANSDUCTION;

EID: 40749099894     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature06667     Document Type: Article

References (18)

1. Warburg, O. On the origin of cancer cells. Science 123, 309-314 (1956).
2. Lum, J. J. et al. The transcription factor HIF-1α plays a critical role in the growth factor-dependent regulation of both aerobic and anaerobic glycolysis. Genes Dev. 21, 1037-1049 (2007).
3. Majumder, P. K. et al. mTOR inhibition reverses Akt-dependent prostate intraepithelial neoplasia through regulation of apoptotic and HIF-1-dependent pathways. Nature Med. 10, 594-601 (2004).
4. Vander Heiden, M. G. et al. Growth factors can influence cell growth and survival through effects on glucose metabolism. Mol. Cell. Biol. 21, 5899-5912 (2001).
5. Eigenbrodt, E., Reinacher, M., Scheefers-Borchel, U., Scheefers, H. & Friis, R. Double role for pyruvate kinase type M2 in the expansion of phosphometabolite pools found in tumor cells. Crit. Rev. Oncog. 3, 91-115 (1992).
6. Zwerschke, W. et al. Modulation of type M2 pyruvate kinase activity by the human papillomavirus type 16 E7 oncoprotein. Proc. Natl Acad. Sci. USA 96, 1291-1296 (1999).
7. Reiss, N., Kanety, H. & Schlessinger, J. Five enzymes of the glycolytic pathway serve as substrates for purified epidermal-growth-factor- receptor kinase. Biochem. J. 239, 691-697 (1986).
8. Sale, E. M., White, M. F. & Kahn, C. R. Phosphorylation of glycolytic and gluconeogenic enzymes by the insulin receptor kinase. J. Cell. Biochem. 33, 15-26 (1987).
9. Presek, P., Reinacher, M. & Eigenbrodt, E. Pyruvate kinase type M2 is phosphorylated at tyrosine residues in cells transformed by Rous sarcoma virus. FEBS Lett. 242, 194-198 (1988).
10. Mazurek, S., Grimm, H., Boschek, C. B., Vaupel, P. & Eigenbrodt, E. Pyruvate kinase type M2: a crossroad in the tumor metabolome. Br. J. Nutr. 87 (suppl. 1), S23-S29 (2002).
11. Ong, S. E. & Mann, M. A practical recipe for stable isotope labeling by amino acids in cell culture (SILAC). Nature Protocols 1, 2650-2660 (2006).
12. Jurica, M. S. et al. The allosteric regulation of pyruvate kinase by fructose-1,6-bisphosphate. Structure 6, 195-210 (1998).
13. Dombrauckas, J. D., Santarsiero, B. D. & Mesecar, A. D. Structural basis for tumor pyruvate kinase M2 allosteric regulation and catalysis. Biochemistry 44, 9417-9429 (2005).
14. Yamada, K. & Noguchi, T. Nutrient and hormonal regulation of pyruvate kinase gene expression. Biochem. J. 337, 1-11 (1999).
15. Villen, J., Beausoleil, S. A., Gerber, S. A. & Gygi, S. P. Large-scale phosphorylation analysis of mouse liver. Proc. Natl Acad. Sci. USA 104, 1488-1493 (2007).
16. Christofk, H. R. et al. The M2 splice isoform of pyruvate kinase is important for cancer metabolism and tumour growth. Nature doi:10.1038/nature06734 (this issue).
17. Hatzivassiliou, G. et al. ATP citrate lyase inhibition can suppress tumor cell growth. Cancer Cell 8, 311-321 (2005).
18. Root, D. E., Hacohen, N., Hahn, W. C., Lander, E. S. & Sabatini, D. M. Genome-scale loss-of-function screening with a lentiviral RNAi library. Nature Methods 3, 715-719 (2006).