A transforming mutation in the pleckstrin homology domain of AKT1 in cancer

Nature

Volumn 448, Issue 7152, 2007, Pages 439-444

  Carpten, John D ^a   Faber, Andrew L ^b   Horn, Candice ^b   Donoho, Gregory P ^b   Briggs, Stephen L ^b   Robbins, Christiane M ^a   Hostetter, Galen ^a   Boguslawski, Sophie ^b   Moses, Tracy Y ^a   Savage, Stephanie ^a   Uhlik, Mark ^b   Lin, Aimin ^b   Du, Jian ^b   Qian, Yue Wei ^b   Zeckner, Douglas J ^b   Tucker Kellogg, Greg ^c   Touchman, Jeffrey ^a   Patel, Ketan ^c   Mousses, Spyro ^a   Bittner, Michael ^a   Schevitz, Richard ^b   Lai, Mei Huei T ^b   Blanchard, Kerry L ^b   Thomas, James E ^b   more..

^a TRANSLATIONAL GENOMICS RESEARCH INSTITUTE   (United States)

^b ELI LILLY AND COMPANY   (United States)

^c Eli Lilly Singapore Pte Ltd   (Singapore)

Author keywords

[No Author keywords available]

Indexed keywords

GLUTAMIC ACID; LIGAND; LIPID BINDING PROTEIN; LYSINE; PHOSPHATIDYLINOSITIDE; PHOSPHATIDYLINOSITOL 3 KINASE; PLECKSTRIN; PROTEIN KINASE B; PROTEIN KINASE B ALPHA; UNCLASSIFIED DRUG;

AMINO ACID; BLOOD SYSTEM DISORDER; CANCER; ENZYME ACTIVITY; HOMOLOGY; MUTATION; RODENT; SIGNALING; WOMENS HEALTH;

ALLOSTERISM; AMINO ACID SUBSTITUTION; ARTICLE; BREAST CANCER; CANCER SURVIVAL; CARCINOGENESIS; CELL MEMBRANE; CELL TRANSFORMATION; COLORECTAL CANCER; CONTROLLED STUDY; DOWNSTREAM PROCESSING; ELECTRICITY; EMBRYO; ENZYME ACTIVATION; ENZYME LOCALIZATION; GENE IDENTIFICATION; GENE MUTATION; HUMAN; HUMAN CELL; HYDROGEN BOND; LEUKEMIA; MOUSE; NONHUMAN; NUCLEOTIDE SEQUENCE; OVARY CANCER; PRIORITY JOURNAL; PROTEIN DOMAIN; SOMATIC MUTATION;

MURINAE; MUS;

EID: 34547172596     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature05933     Document Type: Article

References (37)

1. Vivanco, I. & Sawyers, C. L. The phosphatidylinositol 3-kinase AKT pathway in human cancer. Nature Rev. Cancer 2, 489-501 (2002).
2. Ahmed, N. N. et al. The proteins encoded by c-akt and v-akt differ in post-translational modification, subcellular localization and oncogenic potential. Oncogene 8, 1957-1963 (1993).
3. Bachman, K. E. et al. The PIK3CA gene is mutated with high frequency in human breast cancers. Cancer Biol. Ther. 3, 772-775 (2004).
4. Campbell, I. G. et al. Mutation of the PIK3CA gene in ovarian and breast cancer. Cancer Res. 64, 7678-7681 (2004).
5. Lee, J. W. et al. PIK3CA gene is frequently mutated in breast carcinomas and hepatocellular carcinomas. Oncogene 24, 1477-1480 (2005).
6. Levine, D. A. et al. Frequent mutation of the PIK3CA gene in ovarian and breast cancers. Clin. Cancer Res. 11, 2875-2878 (2005).
7. Saal, L. H. et al. PIK3CA mutations correlate with hormone receptors, node metastasis, and ERBB2, and are mutually exclusive with PTEN loss in human breast carcinoma. Cancer Res. 65, 2554-2559 (2005).
8. Samuels, Y. et al. High frequency of mutations of the PIK3CA gene in human cancers. Science 304, 554 (2004).
9. Cantley, L. C. &Neel, B. G. New insights into tumor suppression: PTEN suppresses tumor formation by restraining the phosphoinositide 3-kinase/AKT pathway. Proc. Natl Acad. Sci. USA 96, 4240-4245 (1999).
10. Khan, S. et al. PTEN promoter is methylated in a proportion of invasive breast cancers. Int. J. Cancer 112, 407-410 (2004).
11. Cantley, L. C. The phosphoinositide 3-kinase pathway. Science 296, 1655-1657 (2002).
12. Stocker, H. et al. Living with lethal PIP3 levels: viability of flies lacking PTEN restored by a PH domain mutation in Akt/PKB. Science 295, 2088-2091 (2002).
13. Fukuda, M., Kojima, T., Kabayama, H. & Mikoshiba, K. Mutation of the pleckstrin homology domain of Bruton's tyrosine kinase in immunodeficiency impaired inositol 1,3,4,5-tetrakisphosphate binding capacity. J. Biol. Chem. 271, 30303-30306 (1996).
14. Franke, T. F. et al. The protein kinase encoded by the Akt proto-oncogene is a target of the PDGF-activated phosphatidylinositol 3-kinase. Cell 81, 727-736 (1995).
15. Li, W., Zhu, T. & Guan, K. L. Transformation potential of Ras isoforms correlates with activation of phosphatidylinositol 3-kinase but not ERK. J. Biol. Chem. 279, 37398-37406 (2004).
16. Andjelkovic, M. et al. Role of translocation in the activation and function of protein kinase B. J. Biol. Chem. 272, 31515-31524 (1997).
17. Mirza, A. M., Kohn, A. D., Roth, R. A. & McMahon, M. Oncogenic transformation of cells by a conditionally active form of the protein kinase Akt/PKB. Cell Growth Differ. 11, 279-292 (2000).
18. Sun, M. et al. AKT1/PKBα kinase is frequently elevated in human cancers and its constitutive activation is required for oncogenic transformation in NIH3T3 cells. Am. J. Pathol. 159, 431-437 (2001).
19. Sjoblom, T. et al. The consensus coding sequences of human breast and colorectal cancers. Science 314, 268-274 (2006).
20. Milburn, C. C. et al. Binding of phosphatidylinositol 3,4,5-trisphosphate to the pleckstrin homology domain of protein kinase B induces a conformational change. Biochem. J. 375, 531-538 (2003).
21. Thomas, C. C., Deak, M., Alessi, D. R. & van Aalten, D. M. High-resolution structure of the pleckstrin homology domain of protein kinase B/Akt bound to phosphatidylinositol (3,4,5)-trisphosphate. Curr. Biol. 12, 1256-1262 (2002).
22. Komander, D. et al. Structural insights into the regulation of PDK1 by phosphoinositides and inositol phosphates. EMBO J. 23, 3918-3928 (2004).
23. Franke, T. F., Kaplan, D. R., Cantley, L. C. & Toker, A. Direct regulation of the Akt proto-oncogene product by phosphatidylinositol-3,4- bisphosphate. Science 275, 665-668 (1997).
24. Klippel, A., Kavanaugh, W. M., Pot, D. & Williams, L. T. A specific product of phosphatidylinositol 3-kinase directly activates the protein kinase Akt through its pleckstrin homology domain. Mol. Cell. Biol. 17, 338-344 (1997).
25. Stephens, L. et al. Protein kinase B kinases that mediate phosphatidylinositol 3,4,5-trisphosphate-dependent activation of protein kinase B. Science 279, 710-714 (1998).
26. Barnett, S. F. et al. Identification and characterization of pleckstrin-homologydomain-dependent and isoenzyme-specific Akt inhibitors. Biochem. J. 385, 399-408 (2005).
27. Watton, S. J. & Downward, J. Akt/PKB localisation and 3′ phosphoinositide generation at sites of epithelial cell-matrix and cell-cell interaction. Curr. Biol. 9, 433-436 (1999).
28. Scheid, M. P., Marignani, P. A. & Woodgett, J. R. Multiple phosphoinositide 3-kinase-dependent steps in activation of protein kinase B. Mol. Cell. Biol. 22, 6247-6260 (2002).
29. Adams, J. M. et al. The c-myc oncogene driven by immunoglobulin enhancers induces lymphoid malignancy in transgenic mice. Nature 318, 533-538 (1985).
30. Wendel, H. G. et al. Survival signalling byAkt and eIF4E in oncogenesis and cancer therapy. Nature 428, 332-337 (2004).
31. Adams, J. M. & Cory, S. Transgenic models for haemopoietic malignancies. Biochim. Biophys. Acta 1072, 9-31 (1991).
32. Altomare, D. A. & Testa, J. R. Perturbations of the AKT signaling pathway in human cancer. Oncogene 24, 7455-7464 (2005).
33. Parsons, D. W. et al. Colorectal cancer: mutations in a signalling pathway. Nature 436, 792 (2005).
34. Staal, S. P. Molecular cloning of the akt oncogene and its human homologues AKT1 and AKT2: amplification of AKT1 in a primary human gastric adenocarcinoma. Proc. Natl Acad. Sci. USA 84, 5034-5037 (1987).
35. Knobbe, C. B. & Reifenberger, G. Genetic alterations and aberrant expression of genes related to the phosphatidyl-inositol-3′-kinase/protein kinase B (Akt) signal transduction pathway in glioblastomas. Brain Pathol. 13, 507-518 (2003).
36. Soung, Y. H. et al. Mutational analysis of AKT1, AKT2 and AKT3 genes in common human carcinomas. Oncology 70, 285-289 (2006).
37. Hawley, R. G. et al. Versatile vectors for potential use in gene therapy. Gene Ther. 1, 136-138 (1994).