Germline KRAS mutations cause Noonan syndrome

Nature Genetics

Volumn 38, Issue 3, 2006, Pages 331-336

  Schubbert, Suzanne ^a   Zenker, Martin ^b   Rowe, Sara L ^a   Böll, Silke ^c   Klein, Cornelia ^c   Bollag, Gideon ^d   Van Der Burgt, Ineke ^e   Musante, Luciana ^f   Kalscheuer, Vera ^f   Wehner, Lars Erik ^g   Nguyen, Hoa ^d   West, Brian ^d   Zhang, Kam Y J ^d   Sistermans, Erik ^e   Rauch, Anita ^b   Niemeyer, Charlotte M ^c   Shannon, Kevin ^a,h   Kratz, Christian P ^c  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b UNIVERSITY OF ERLANGEN NUREMBERG   (Germany)

^c UNIVERSITY OF FREIBURG   (Germany)

^d PLEXXIKON INC   (United States)

^e RADBOUD UNIVERSITY MEDICAL CENTER   (Netherlands)

^f MAX PLANCK INSTITUTE FOR MOLECULAR GENETICS   (Germany)

^g UNIVERSITY OF GÖTTINGEN   (Germany)

^h UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

GROWTH FACTOR; GUANOSINE TRIPHOSPHATASE ACTIVATING PROTEIN; GUANOSINE TRIPHOSPHATE; K RAS PROTEIN; RECOMBINANT PROTEIN;

ADOLESCENT; ADULT; AMINO ACID SUBSTITUTION; ANIMAL CELL; ARTICLE; CARDIO FACIOCUTANEOUS SYNDROME; CELL LINEAGE; CLINICAL ARTICLE; CLINICAL FEATURE; FEMALE; GENE MUTATION; GENETIC DISORDER; HEMATOPOIETIC STEM CELL; HUMAN; HUMAN CELL; HYPERSENSITIVITY; MALE; MOUSE; NONHUMAN; NOONAN SYNDROME; PRESCHOOL CHILD; PRIORITY JOURNAL; PROTEIN HYDROLYSIS; SIGNAL TRANSDUCTION; STEM CELL;

ADOLESCENT; FEMALE; GENES, RAS; GERM-LINE MUTATION; GUANOSINE TRIPHOSPHATE; HETEROZYGOTE DETECTION; HUMANS; INFANT; INTRACELLULAR SIGNALING PEPTIDES AND PROTEINS; MALE; NOONAN SYNDROME; PROTEIN-TYROSINE-PHOSPHATASE;

ANIMALIA;

EID: 33644622238     PISSN: 10614036     EISSN: None     Source Type: Journal    
DOI: 10.1038/ng1748     Document Type: Article

References (30)

1. Tartaglia, M. & Gelb, B.D. Noonan syndrome and related disorders: genetics and pathogenesis. Annu. Rev. Genomics Hum. Genet. 6, 45-68 (2005).
2. Tartaglia, M. et al. Mutations in PTPN11, encoding the protein tyrosine phosphatase SHP-2, cause Noonan syndrome. Nat. Genet. 29, 465-468 (2001).
3. Neel, B.G., Gu, H. & Pao, L. The 'Shp'ing news: SH2 domain-containing tyrosine phosphatases in cell signaling. Trends Biochem. Sci. 28, 284-293 (2003).
4. Kavamura, M.I., Peres, C.A., Alchorne, M.M. & Brunoni, D. CFC index for the diagnosis of cardiofaciocutaneous syndrome. Am. J. Med. Genet. 112, 12-16 (2002).
5. Vetter, I.R. & Wittinghofer, A. The guanine nucleotide-binding switch in three dimensions. Science 294, 1299-1304 (2001).
6. Donovan, S., Shannon, K.M. & Bollag, G. GTPase activating proteins: critical regulators of intracellular signaling. Biochim. Biophys. Acta 1602, 23-45 (2002).
7. Bos, J.L. ras oncogenes in human cancer: a review. Cancer Res. 49, 4682-4689 (1989).
8. Lauchle, J.O., Braun, B.S., Loh, M.L. & Shannon, K. Inherited predispositions and hyperactive Ras in myeloid leukemogenesis. Pediatr. Blood Cancer (2005).
9. Bollag, G. et al. Loss of NF1 results in activation of the Ras signaling pathway and leads to aberrant growth in murine and human hematopoietic cells. Nat. Genet. 12, 144-148 (1996).
10. Side, L. et al. Homozygous inactivation of the NF1 gene in bone marrow cells from children with neurofibromatosis type 1 and malignant myeloid disorders. N. Engl. J. Med. 336, 1713-1720 (1997).
11. Tartaglia, M. et al. Somatic mutations in PTPN11 in juvenile myelomonocytic leukemia, myelodysplastic syndromes and acute myeloid leukemia. Nat. Genet. 34, 148-150 (2003).
12. Kratz, C.P. et al. The mutational spectrum of PTPN11 in juvenile myelomonocytic leukemia and Noonan syndrome/myeloproliferative disease. Blood 106, 2183-2185 (2005).
13. Keilhack, H., David, F.S., McGregor, M., Cantley, L.C. & Neel, B.G. Diverse biochemical properties of Shp2 mutants: Implications for disease phenotypes. J. Biol. Chem. 280, 30984-30993 (2005).
14. Mohi, M.G. et al. Prognostic, therapeutic, and mechanistic implications of a mouse model of leukemia evoked by Shp2 (PTPN11) mutations. Cancer Cell 7, 179-191 (2005).
15. Chan, R.J. et al. Human somatic PTPN11 mutations induce hematopoietic-cell hypersensitivity to granulocyte-macrophage colony-stimulating factor. Blood 105, 3737-3742 (2005).
16. Schubbert, S. et al. Functional analysis of leukemia-associated PTPN11 mutations in primary hematopoietic cells. Blood 106, 311-317 (2005).
17. Bollag, G. et al. Biochemical characterization of a novel KRAS insertional mutation from a human leukemia. J. Biol. Chem. 273, 32491-32494 (1996).
18. Bollag, G. & McCormick, F. Differential regulation of rasGAP and neurofibromatosis gene product activities. Nature 351, 576-579 (1991).
19. Serrano, M., Lin, A.W., McCurrach, M.E., Beach, D. & Lowe, S.W. Oncogenic ras provokes premature cell senescence associated with accumulation of p53 and p16INK4a. Cell 88, 593-602 (1997).
20. Aoki, Y. et al. Germline mutations in HRAS proto-oncogene cause Costello syndrome. Nat. Genet. 37, 1038-1040 (2005).
21. Tuveson, D.A. et al. Endogenous oncogenic K-ras(G12D) stimulates proliferation and widespread neoplastic and developmental defects. Cancer Cell 5, 375-387 (2004).
22. Johnson, L. et al. K-ras is an essential gene in the mouse with partial functional overlap with N-ras. Genes Dev. 11, 2468-2481 (1997).
23. Marshall, C. Specificity of receptor tyrosine kinase signaling: transient versus sustained extracellular signal-regulated kinase activation. Cell 80, 179-185 (1995).
24. Franken, S.M. et al. Three-dimensional structures and properties of a transforming and a nontransforming glycine-12 mutant of p21H-ras. Biochemistry 32, 8411-8420 (1993).
25. Largaespada, D.A., Brannan, C.I., Jenkins, N.A. & Copeland, N.G. Nf1 deficiency causes Ras-mediated granulocyte-macrophage colony stimulating factor hypersensitivity and chronic myeloid leukemia. Nat. Genet. 12, 137-143 (1996).
26. Hiatt, K.K., Ingram, D.A., Zhang, Y., Bollag, G. & Clapp, D.W. Neurofibromin GTPase-activating protein-related domains restore normal growth in Nf1-/- cells. J. Biol. Chem. 276, 7240-7245 (2001).
27. Stone, J.C., Colleton, M. & Bottorff, D. Effector domain mutations dissociate p21ras effector function and GTPase-activating protein interaction. Mol. Cell. Biol. 13, 7311-7320 (1993).
28. Araki, T. et al. Mouse model of Noonan syndrome reveals cell type- and gene dosage-dependent effects of Ptpn11 mutation. Nat. Med. 10, 849-857 (2004).
29. Zenker, M. et al. Genotype-phenotype correlations in Noonan syndrome. J. Pediatr. 144, 368-374 (2004).
30. Donovan, S., See, W., Bonifas, J., Stokoe, D. & Shannon, K.M. Hyperactivation of protein kinase B and ERK have discrete effects on survival, proliferation, and cytokine expression in Nf1-deficient myeloid cells. Cancer Cell 2, 507-514 (2002).