Identification of a 14-3-3 binding sequence in the common β chain of the granulocyte-macrophage colony-stimulating factor (GM-CSF), interleukin-3 (IL-3), and IL-5 receptors that is serine-phosphorylated by GM-CSF

Blood

Volumn 94, Issue 6, 1999, Pages 1933-1942

  Stomski, F C ^b   Dottore, M ^b   Winnall, W ^b   Guthridge, M A ^b   Woodcock, J ^b   Bagley, C J ^b   Thomas, D T ^b   Andrews, R K ^b   Berndt, M C ^b   Lopez, A F ^a  

^a INSTITUTE OF MEDICAL AND VETERINARY SCIENCE   (Australia)

^b NONE

Author keywords

[No Author keywords available]

Indexed keywords

ADAPTOR PROTEIN; GLUTATHIONE TRANSFERASE; GRANULOCYTE MACROPHAGE COLONY STIMULATING FACTOR; GRANULOCYTE MACROPHAGE COLONY STIMULATING FACTOR RECEPTOR; HYBRID PROTEIN; INTERLEUKIN 3; INTERLEUKIN 3 RECEPTOR; INTERLEUKIN 5; INTERLEUKIN 5 RECEPTOR;

ARTICLE; HUMAN; HUMAN CELL; LEUKEMIA CELL LINE; PRIORITY JOURNAL; PROTEIN PHOSPHORYLATION; RECEPTOR BINDING;

EID: 0033568169     PISSN: 00064971     EISSN: None     Source Type: Journal    
DOI: 10.1182/blood.v94.6.1933     Document Type: Article

References (53)

1. Sanderson CJ: Interleukin-5, eosinophils, and disease. Blood 79:3101, 1992
2. Metcalf D: The molecular biology and functions of the granulocyte-macrophage colony-stimulating factors. Blood 67:257, 1986
3. Metcalf D: The molecular control of cell division, differentiation commitment and maturation in haemopoietic cells. Nature 339:27, 1989
4. Clark SC, Kamen R: The human hematopoietic colony-stimulating factors. Science 236:1229, 1987
5. Kitamura T, Sato N, Arai K, Miyajima A: Expression cloning of the human IL-3 receptor cDNA reveals a shared β subunit for the human IL-3 and GM-CSF receptors. Cell 66:1165, 1991
6. Tavernier J, Devos R, Cornelis S, Tuypens T, Van der Heyden J, Fiers W, Plaetinck G: A human high affinity interleukin-5 receptor (IL5R) is composed of an IL5-specific a chain and a β chain shared with the receptor for GM-CSF. Cell 66:1175, 1991
7. Hayashida K, Kitamura T, Gorman DM, Arai K, Yokota T, Miyajima A: Molecular cloning of a second subunit of the receptor for human granulocyte-macrophage colony-stimulating factor (GM-CSF): Reconstitution of a high-affinity GM-CSF receptor. Proc Natl Acad Sci USA 87:9655, 1990
8. Nicola NA: Guidebook to Cytokines and Their Receptors. Sambrook, Tooze (eds): Oxford, UK, Oxford, 1994
9. Miyajima A, Kinoshita T, Wakao H, Hara T, Yoshimura A, Nishinakamura R, Murray R, Mui A: Signal transduction by the GM-CSF, IL-3 and IL-5 receptors. Leukemia 11:418, 1997 (suppl 3)
10. Gobert S, Chretien S, Gouilleux F, Muller O, Pallard C, Dusanter-Fourt I, Gronar B, Lacombe C, Gisselbrecht S, Mayeux P: Identification of tyrosine residues within the intracellular domain of the erythropoietin receptor crucial for STATS activation. EMBO J 15:2434, 1996
11. Murakami M, Hibi M, Nakagawa N, Nakagawa T, Yasakawa K, Yamanishi K, Taga T, Kishimoto T: IL-6 induced homodimerisation of gp130 and associated activation of a tyrosine kinase. Science 260:1808, 1993
12. Heldin C-H: Dimerization of cell surface receptors in signal transduction. Cell 80:213, 1995
13. Nakamura Y, Russell SM, Mess SA, Friedmann M, Erdos M, Francois C, Jacques Y, Adelstein S, Leonard WJ: Heterodimerization of the IL-2 receptor beta- and gamma-chain cytoplasmic domains is required for signalling. Nature 369:330, 1994
14. Muto A, Watanabe S, Miyajima A, Yokota T, Arai K-I: The β subunit of human granulocyte-macrophage colony-stimulating factor receptor forms a homodimer and is activated via association with the α subunit. J Exp Med 183:1911, 1996
15. Mui AL-F, Wakao H, O'Farrell A-M, Harada N, Miyajima A: Interleukin-3, granulocyte-macrophage colony stimulating factor and interleukin-5 transduce signals through two STAT5 homologs. EMBO J 14:1166, 1995
16. Itoh T, Liu R, Yokota T, Arai K, Watanabe S: Definition of the role of tyrosine residues of the common beta subunit regulating multiple signaling pathways of granulocyte-macrophage colony-stimulating factor receptor. Mol Cell Biol 18:742, 1998
17. Okuda K, Smith L, Griffin JD, Foster R: Signaling functions of the tyrosine residues in the βc chain of the granulocyte-macrophage colony-stimulating factor receptor. Blood 90:4759, 1997
18. Itoh T, Muto A, Watanabe S, Miyajima A, Yokota T, Arai K: Granulocyte-macrophage colony-stimulating factor provokes RAS activation and transcription of c-fos through different modes of signaling. J Biol Chem 271:7587, 1996
19. Durstin M, Inhom RC, Griffin JD: Tyrosine phosphorylation of She is not required for proliferation or viability signaling by granulocyte-macrophage colony-stimulating factor in hematopoietic cell lines. J Immunol 157:534, 1996
20. Sato N, Sakamaki K, Terada N, Arai K, Miyajima A: Signal transduction by the high affinity GM-CSF receptor: Two distinct cytoplasmic regions of the common β subunit responsible for different signalling. EMBO J 12:4181, 1993
21. Gale RE, Freeburn RW, Khwaja A, Copra R, Linch DC: A truncated isoform of the human β chain common to the receptors for granulocyte-macrophage colony-stimulating factor, interleukin-3 (IL-3), and IL-5 with increased mRNA expression n some patients with acute leukemia. Blood 91:54, 1998
22. Drachman JG, Kaushansky K: Dissecting the thrombopoietin receptor: Functional elements of the Mp1 cytoplasmic domain. Proc Natl Acad Sci USA 94:2350, 1997
23. Longmore GD, You Y, Molden J, Liu KD, Mikami A, Lai SY, Pharr P, Goldsmith MA: Redundant and selective roles for erythropoietin receptor tyrosines in erythropoiesis in vivo. Blood 91:870, 1998
24. Teglund S, McKay C, Schuetz E, van Deursen JM, Stravopodis D, Wang D, Brown M, Bodner S, Grosveld G, Ihle JN: Stat5a and Stat5b proteins have essential and nonessential, or redundant, roles in cytokine responses. Cell 93:841, 1998
25. Guthridge MA, Stomski FC, Thomas DT, Woodcock JM, Bagley CJ, Berndt MC, Lopez AF: Mechanism of activation of the GM-CSF, IL-3, and IL-5 family of receptors. Stem Cells 16:301, 1998
26. 21 of GM-CSF. EMBO J 13:5176, 1994
27. 22, selectively interact with the α- and β-chains of its receptor and participate in function. J Biol Chem 269:8488, 1994
28. Hercus TR, Bagley CJ, Cambareri B, Dottore M, Woodcock JM, Vadas MA, Shannon MF, Lopez AF: Specific human granulocyte-macrophage colony-stimulating factor antagonists. Proc Natl Acad Sci USA 91:5838, 1994
29. Kitamura T, Tange T, Terasawa T, Chiba S, Kuwaki K, Miyagawa K, Piao Y-F, Miyazano K, Urabe A, Takaku F: Establishment and characterization of a unique human cell line that proliferates dependently on GM-CSF, IL-3, or erythropoietin. J Cell Physiol 140:323, 1989
30. Stomski FC, Woodcock JM, Zacharakis B, Bagley CJ, Sun Q, Lopez AF: Identification of a Cys motif in the common β chain of the IL-3, GM-CSF and IL-5 receptors essential for disulfide-linked receptor heterodimerization and activation of all three receptors. J Biol Chem 273:1192, 1998
31. Graham FL, van der Eb AJ: A new technique for the assay of infectivity of human adenovirus 5 DNA. Virology 52:456, 1973
32. Stomski FC, Sun Q, Bagley CJ, Woodcock JM, Goodall GJ, Andrews RK, Berndt MC, Lopez AF: Human interleukin-3 (IL-3) induces disulphide-linked receptor a and β chain heterodimerization which is required for receptor activation but not high affinity binding. Mol Cell Biol 16:3035, 1996
33. Martin H, Rostas J, Patel Y, Aitken A: Subcellular localisation of 14-3-3 isoforms in rat brain using specific antibodies. J Neurochem 63:2259, 1994
34. Smith A, Metcalf D, Nicola NA: Cytoplasmic domains of the common β-chain of the GM-CSF/IL-3/IL-5 receptors that are required for inducing differentiation or clonal suppression in myeloid leukaemic cell lines. EMBO J 16:451, 1997
35. Muslin AJ, Tanner JW, Allen PM, Shaw AS: Interaction of 14-3-3 with signaling proteins is mediated by the recognition of phosphoserine. Cell 84:889, 1996
36. Yaffe MB, Rittinger K, Volinia S, Caron PR, Aitken A, Leffers H, Gamblin SJ, Smerfon SJ, Cantley LC: The structural basis for 14-3-3: phosphopeptide binding specificity. Cell 91:961, 1997
37. Bone H, Dechert U, Jirik F, Schrader JW, Welham MJ: SHP1 and SHP2 protein-tyrosine phosphatases associate with betac after interleukin-3-induced receptor tyrosine phosphorylation. Identification of potential binding sites and substrates. J Biol Chem 272:14470, 1997
38. Aitken A: 14-3-3 proteins on the MAP. Trends Biochem Sci 20:95, 1995
39. Aitken A, Jones D, Soneji Y, Howell S: 14-3-3 proteins: Biological function and domain structure. Biochem Soci Trans 23:605, 1995
40. Luo Z, Zhang X, Rapp U, Avruch J: Identification of the 14.3.3 zeta domains important for self-association and Raf binding. J Biol Chem 270:23681, 1995
41. Braselmann S, McCormack F: Bcr and Raf form a complex in vivo via 14-3-3 proteins. EMBO J 14:4839, 1995
42. Liu YC, Liu Y, Elly C, Yoshida H, Lipkowitz S, Altman A: Serine phosphorylation of Cbl induced by phorbol ester enhances its association with 14-3-3 proteins in T cells via a novel serine-rich 14-3-3-binding motif. J Biol Chem 272:9979, 1997
43. Zhang SH, Kobayashi R, Graves PR, Piwnica-Worms H, Tonks NK: Serine phosphorylation-dependent association of the band 4.1-related protein-tyrosine phosphatase PTPH1 with 14-3-3 β protein. J Biol Chem 272:27281, 1997
44. Kumagai A, Yakowec PS, Dunphy WG: 14-3-3 proteins act as negative regulators of the mitotic inducer Cdc25 in Xenopus egg extracts. Mol Biol Cell 9:345, 1998
45. Craparo A, Freund R, Gustafson TA: 14-3-3 (epsilon) interacts with the insulin-like growth factor I receptor and insulin receptor substrate I in a phosphoserine-dependent manner. J Biol Chem 272: 11663, 1997
46. Ogihara T, Isobe T, Ichimaru T, Taoka M, Funaki M, Sakoda H, Onishi Y, Inukai K, Anai M, Fukushima Y, Kikuchi M, Yazaki Y, Oka Y, Asano T: 14-3-3 protein binds to insulin receptor substrate-1, one of the binding sites of which is in the phosphotyrosine binding domain. J Biol Chem 272:25267, 1997
47. Wakui H, Wright AP, Gustafsson J, Zilliacus J: Interaction of the ligand-activated glucocorticoid receptor with the 14-3-3 eta protein. J Biol Chem 272:8153, 1997
48. Meller N, Liu YC, Collins TL, Bonnefoy-Berard N, Baier G, Isakov N, Altman A: Direct interaction between protein kinase C theta (PKC theta) and 14-3-3 tau in T cells: 14-3-3 overexpression results in inhibition of PKC theta translocation and function. Mol Cell Biol 16:5782, 1996
49. L. Cell 87:519, 1996
50. Fanger GR, Widmann C, Porter AC, Sather S, Johnson GL, Vaillancourt RR: 14-3-3 proteins interact with specific MEK kinases. J Biol Chem 273:3476, 1998
51. Liu D, Bienkowska J, Petosa C, Collier RJ, Fu H, Liddington R: Crystal structure of the zeta isoform of the 14-3-3 protein. Nature 376:191, 1995
52. Xiao B, Smerdon SJ, Jones DH, Dodson GG, Soneji Y, Aitken A, Gamblin SJ: Structure of a 14-3-3 protein and implications for coordination of multiple signalling pathways. Nature 376:188, 1995
53. Vincenz C, Dixit VM: 14-3-3 proteins associate with A20 in an isoform-specific manner and function both as chaperone and adapter molecules. J Biol Chem 271:20029, 1996