Lnk adaptor suppresses radiation resistance and radiation-induced B-cell malignancies by inhibiting IL-11 signaling

Proceedings of the National Academy of Sciences of the United States of America

Volumn 110, Issue 51, 2013, Pages 20599-20604

  Louria Hayon, Igal ^a   Frelin, Catherine ^b   Ruston, Julie ^a   Gish, Gerald ^a   Jin, Jing ^a   Kofler, Michael M ^a   Lambert, Jean Philippe ^a   Adissu, Hibret A ^c   Milyavsky, Michael ^b,d   Herrington, Robert ^b   Minden, Mark D ^b   Dick, John E ^b,d   Gingras, Anne Claude ^a   Iscove, Norman N ^b   Pawson, Tony ^a,d  

^a MOUNT SINAI HOSPITAL   (Canada)

^b PRINCESS MARGARET HOSPITAL   (Canada)

^c Toronto Centre for Phenogenomics   (Canada)

^d UNIVERSITY OF TORONTO   (Canada)

Author keywords

Cancer; Gp130; Lymphoma; Survival

Indexed keywords

ADAPTOR PROTEIN; CD135 ANTIGEN; INTERLEUKIN 11; LNK ADAPTOR PROTEIN; MITOGEN ACTIVATED PROTEIN KINASE; PROTEIN TYROSINE PHOSPHATASE SHP 2; UNCLASSIFIED DRUG;

ACUTE LYMPHOBLASTIC LEUKEMIA; ANIMAL CELL; ANIMAL TISSUE; ARTICLE; B CELL LYMPHOMA; B CELL MALIGNANCY; B LYMPHOCYTE; FLOW CYTOMETRY; GAMMA IRRADIATION; HEMATOLOGIC MALIGNANCY; HEMATOPOIETIC STEM CELL; IN VIVO STUDY; MOUSE; NONHUMAN; PEPTIDE SYNTHESIS; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN PHOSPHORYLATION; RADIATION INJURY; RADIOSENSITIVITY; SIGNAL TRANSDUCTION;

EID: 84890817543     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1319665110     Document Type: Article

References (39)

1. Newhauser WD, Durante M (2011) Assessing the risk of second malignancies after modern radiotherapy. Nat Rev Cancer 11(6):438-448.
2. Grivennikov SI, Greten FR, Karin M (2010) Immunity, inflammation, and cancer. Cell 140(6):883-899.
3. Vainchenker W, Constantinescu SN (2013) JAK/STAT signaling in hematological malignancies. Oncogene 32(21):2601-2613.
4. Li Y, He X, Schembri-King J, Jakes S, Hayashi J (2000) Cloning and characterization of human Lnk, an adaptor protein with pleckstrin homology and Src homology 2 domains that can inhibit T cell activation. J Immunol 164(10):5199-5206.
5. Takaki S, et al. (2000) Control of B cell production by the adaptor protein lnk. Definition of a conserved family of signal-Modulating proteins. Immunity 13(5):599-609.
6. Velazquez L, et al. (2002) Cytokine signaling and hematopoietic homeostasis are disrupted in Lnk-Deficient mice. J Exp Med 195(12):1599-1611.
7. Tong W, Zhang J, Lodish HF (2005) Lnk inhibits erythropoiesis and Epo-Dependent JAK2 activation and downstream signaling pathways. Blood 105(12):4604-4612.
8. Buza-Vidas N, et al. (2006) Cytokines regulate postnatal hematopoietic stem cell expansion: Opposing roles of thrombopoietin and LNK. Genes Dev 20(15):2018-2023.
9. Bersenev A, Wu C, Balcerek J, Tong W (2008) Lnk controls mouse hematopoietic stem cell self-Renewal and quiescence through direct interactions with JAK2. J Clin Invest 118(8):2832-2844.
10. Ema H, et al. (2005) Quantification of self-Renewal capacity in single hematopoietic stem cells from normal and Lnk-Deficient mice. Dev Cell 8(6):907-914.
11. Seita J, et al. (2007) Lnk negatively regulates self-Renewal of hematopoietic stem cells by modifying thrombopoietin-Mediated signal transduction. Proc Natl Acad Sci USA 104(7):2349-2354.
12. Bersenev A, et al. (2010) Lnk constrains myeloproliferative diseases in mice. J Clin Invest 120(6):2058-2069.
13. Oh ST, et al. (2010) Novel mutations in the inhibitory adaptor protein LNK drive JAKSTAT signaling in patients with myeloproliferative neoplasms. Blood 116(6):988-992.
14. Pardanani A, et al. (2010) LNK mutation studies in blast-Phase myeloproliferative neoplasms, and in chronic-Phase disease with TET2, IDH, JAK2 or MPL mutations. Leukemia 24(10):1713-1718.
15. Roberts KG, et al. (2012) Genetic alterations activating kinase and cytokine receptor signaling in high-Risk acute lymphoblastic leukemia. Cancer Cell 22(2):153-166.
16. Zhang J, et al. (2012) The genetic basis of early T-Cell precursor acute lymphoblastic leukaemia. Nature 481(7380):157-163.
17. Milyavsky M, et al. (2010) A distinctive DNA damage response in human hematopoietic stem cells reveals an apoptosis-Independent role for p53 in self-Renewal. Cell Stem Cell 7(2):186-197.
18. Benveniste P, et al. (2010) Intermediate-Term hematopoietic stem cells with extended but time-Limited reconstitution potential. Cell Stem Cell 6(1):48-58.
19. Taga T, Kishimoto T (1997) Gp130 and the interleukin-6 family of cytokines. Annu Rev Immunol 15:797-819.
20. Neddermann P, Graziani R, Ciliberto G, Paonessa G (1996) Functional expression of soluble human interleukin-11 (IL-11) receptor alpha and stoichiometry of in vitro IL-11 receptor complexes with gp130. J Biol Chem 271(48):30986-30991.
21. Murakami M, et al. (1993) IL-6-Induced homodimerization of gp130 and associated activation of a tyrosine kinase. Science 260(5115):1808-1810.
22. Yin T, Shen R, Feng GS, Yang YC (1997) Molecular characterization of specific interactions between SHP-2 phosphatase and JAK tyrosine kinases. J Biol Chem 272(2): 1032-1037.
23. Vogel W, Ullrich A (1996) Multiple in vivo phosphorylated tyrosine phosphatase SHP-2 engages binding to Grb2 via tyrosinee. Cell Growth Differ 7(12): 1589-1597.
24. Kim H, Baumann H (1999) Dual signaling role of the protein tyrosine phosphatase SHP-2 in regulating expression of acute-Phase plasma proteins by interleukin-6 cytokine receptors in hepatic cells. Mol Cell Biol 19(8):5326-5338.
25. Saxton TM, et al. (2000) The SH2 tyrosine phosphatase shp2 is required for mammalian limb development. Nat Genet 24(4):420-423.
26. Qu CK, et al. (1998) Biased suppression of hematopoiesis and multiple developmental defects in chimeric mice containing Shp-2 mutant cells. Mol Cell Biol 18(10): 6075-6082.
27. Chan G, et al. (2011) Essential role for Ptpn11 in survival of hematopoietic stem and progenitor cells. Blood 117(16):4253-4261.
28. Tartaglia M, et al. (2001) Mutations in PTPN11, encoding the protein tyrosine phosphatase SHP-2, cause Noonan syndrome. Nat Genet 29(4):465-468.
29. Legius E, et al. (2002) PTPN11 mutations in LEOPARD syndrome. J Med Genet 39(8): 571-574.
30. Chan RJ, Feng GS (2007) PTPN11 is the first identified proto-Oncogene that encodes a tyrosine phosphatase. Blood 109(3):862-867.
31. Chan G, et al. (2009) Leukemogenic Ptpn11 causes fatal myeloproliferative disorder via cell-Autonomous effects on multiple stages of hematopoiesis. Blood 113(18): 4414-4424.
32. Xu D, et al. (2010) A germline gain-Of-Function mutation in Ptpn11 (Shp-2) phosphatase induces myeloproliferative disease by aberrant activation of hematopoietic stem cells. Blood 116(18):3611-3621.
33. Wiesner S, et al. (2006) A change in conformational dynamics underlies the activation of Eph receptor tyrosine kinases. EMBO J 25(19):4686-4696.
34. Martinelli S, et al. (2012) Counteracting effects operating on Src homology 2 domaincontaining protein-Tyrosine phosphatase 2 (SHP2) function drive selection of the recurrent Y62D and Y63C substitutions in Noonan syndrome. J Biol Chem 287(32): 27066-27077.
35. Van der Meeren A, Mouthon MA, Gaugler MH, Vandamme M, Gourmelon P (2002) Administration of recombinant human IL11 after supralethal radiation exposure promotes survival in mice: Interactive effect with thrombopoietin. Radiat Res 157(6): 642-649.
36. Lapidot T, et al. (1994) A cell initiating human acute myeloid leukaemia after transplantation into SCID mice. Nature 367(6464):645-648.
37. Eppert K, et al. (2011) Stem cell gene expression programs influence clinical outcome in human leukemia. Nat Med 17(9):1086-1093.
38. Jin J, Woodgett JR (2005) Chronic activation of protein kinase Bbeta/Akt2 leads to multinucleation and cell fusion in human epithelial kidney cells: Events associated with tumorigenesis. Oncogene 24(35):5459-5470.
39. Filippakopoulos P, et al. (2008) Structural coupling of SH2-Kinase domains links Fes and Abl substrate recognition and kinase activation. Cell 134(5):793-803.