The JAK-binding protein JAB inhibits Janus tyrosine kinase activity through binding in the activation loop

EMBO Journal

Volumn 18, Issue 5, 1999, Pages 1309-1320

  Yasukawa, Hideo ^a,b   Misawa, Hiroyuki ^a,c   Sakamoto, Hiroshi ^a   Masuhara, Masaaki ^a   Sasaki, Atsuo ^a   Wakioka, Toru ^a   Ohtsuka, Satoshi ^a   Imaizumi, Tsutomu ^b   Matsuda, Tadashi ^d,e   Ihle, James N ^d   Yoshimura, Akihiko ^a  

^a KURUME UNIVERSITY   (Japan)

^b KURUME UNIVERSITY SCHOOL OF MEDICINE   (Japan)

^c UNIVERSITY OF SHIZUOKA   (Japan)

^d ST JUDE CHILDREN S RESEARCH HOSPITAL   (United States)

^e UNIVERSITY OF TOYAMA   (Japan)

Author keywords

Activation loop; CIS; JAB; JAK; SH2 domain

Indexed keywords

BINDING PROTEIN; CYTOKINE RECEPTOR; ISOLEUCINE; LEUCINE; PROTEIN TYROSINE KINASE; PROTEIN TYROSINE KINASE INHIBITOR;

AMINO TERMINAL SEQUENCE; ARTICLE; CELL DIFFERENTIATION; CELL GROWTH; HUMAN; HUMAN CELL; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN FAMILY; PROTEIN PHOSPHORYLATION;

EID: 20244389693     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/18.5.1309     Document Type: Article

References (39)

1. Adams, T.E., Hansen, J.A., Starr, R., Nicola, N.A., Hilton, D.J. and Billestrup, N. (1998) Growth hormone preferentially induces the rapid, transient expression of SOCS-3, a novel inhibitor of cytokine receptor signaling. J. Biol. Chem., 273, 1285-1287.
2. Aman, M.J. and Leonard, W.J. (1997) Cytokine signaling: cytokine-inducible signaling inhibitors. Curr. Biol., 7, 784-788.
3. Becker, S., Groner, B. and Muller, C.W. (1998) Three-dimensional structure of the Stat3β homodimer bound to DNA. Nature, 394, 145-151.
4. Bjorbaek, C., Elmquist, J.K., Frantz, J.D., Shoelson, S.E. and Flier, J.S. (1998) Identification of SOCS-3 as a potential mediator of central leptin resistance. Mol. Cell, 4, 619-625.
5. Brotherton, D.H. et al. (1998) Crystal structure of the complex of the cyclin D-dependent kinase Cdk6 bound to the cell-cycle inhibitor p19INK4d. Nature, 395, 244-250.
6. Chen, X., Vinkemeier, U., Zhao, Y., Jeruzalmi, D., Darnell, J.E.Jr and Kuriyan, J. (1998) Crystal structure of a tyrosine phosphorylated STAT-1 dimer bound to DNA. Cell, 93, 827-839.
7. Cheng, H.C., Van Patten, S.M., Smith, A.J. and Walsh, D.A. (1985) An active twenty-amino-acid-residue peptide derived from the inhibitor protein of the cyclic AMP-dependent protein kinase. Biochem. J., 231, 655-661.
8. Cheng, H.C., Kemp, B.E., Pearson, R.B., Smith, A.J., Misconi, L., Van Patten, S.M. and Walsh, D.A. (1986) A potent synthetic peptide inhibitor of the cAMP-dependent protein kinase. J. Biol. Chem., 261, 989-992.
9. Darnell, J.E.Jr (1997) STATs and gene regulation. Science, 277, 1630-1635.
10. Endo, T.A. et al. (1997) A new protein containing an SH2 domain that inhibits JAK kinases. Nature, 387, 921-924.
11. Feng, J., Witthuhn, B.A., Matsuda, T., Kohlhuber, F., Kerr, I.M. and Ihle, J.N. (1997) Activation of Jak2 catalytic activity requires phosphorylation of Y1007 in the kinase activation loop. Mol. Cell. Biol., 17, 2497-2501.
12. Gauzzi, M.C. Velazquez, L., McKendry, R., Mogensen, K.E., Fellous, M. and Pellegrini, S. (1996) Interferon-alpha-dependent activation of Tyk2 requires phosphorylation of positive regulatory tyrosines by another kinase. J. Biol. Chem., 271, 20494-20500.
13. He, W., Rose, D.W., Olefsky, J.M. and Gustafson, T.A. (1998) Grb10 interacts differentially with the insulin receptor, insulin-like growth factor I receptor and epidermal growth factor receptor via the Grb10 Src homology 2 (SH2) domain and a second novel domain located between the pleckstrin homology and SH2 domains. J. Biol. Chem., 273, 6860-6867.
14. Hilton, D.J. et al. (1998) Twenty proteins containing a C-terminal SOCS box form five structural classes. Proc. Natl Acad. Sci. USA, 95, 114-119.
15. House, C. and Kemp, B.E. (1987) Protein kinase C contains a pseudosubstrate prototope in its regulatory domain. Science, 238, 1726-1728.
16. Ihle, J.N. (1995) Cytokine receptor signaling. Nature, 377, 591-594.
17. Ihle, J.N. (1996) STATs: signal transducers and activators of transcription. Cell, 84, 331-334.
18. Jiao, H., Berrada, K., Yang, W., Tabrizi, M., Platanias, L.C. and Yi, T. (1996) Direct association with and dephosphorylation of Jak2 kinase by the SH2-domain-containing protein tyrosine phosphatase SHP-1. Mol. Cell. Biol., 16, 6985-6992.
19. Kasus-Jacobi, A., Perdereau, D., Auzan, C., Clauser, E., Van Obberghen, E., Mauvais-Jarvis, F., Girard, J., and Burnol, A. (1998) Identification of the rat adapter Grb14 as an inhibitor of insulin actions. J. Biol. Chem., 273, 26026-26035.
20. Klingmuller, U., Lorenz, U., Cantley, L.C., Neel, B.G. and Lodish, H.F. (1995). Specific recruitment of SH-PTP1 to the erythropoietin receptor causes inactivation of JAK2 and termination of proliferative signals. Cell, 80, 729-738.
21. Knighton, D.R., Zheng, J.H., Ten Eyck, L.F., Xuong, N.H., Taylor, S.S. and Sowadski, J.M. (1991). Structure of a peptide inhibitor bound to the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase. Science, 253, 414-420.
22. Kozlowski, M., Larose, L., Lee, F., Le, D.M., Rottapel, R. and Siminovitch, K.A. (1998) SHP-1 binds and negatively modulates the c-Kit receptor by interaction with tyrosine 569 in the c-Kit juxtamembrane domain. Mol. Cell. Biol., 18, 2089-2099.
23. Liu, K.D., Gaffen, S.L., Goldsmith, M.A. and Greene, W.C. (1997) Janus kinases in interleukin-2-mediated signaling: JAK1 and JAK3 are differentially regulated by tyrosine phosphorylation. Curr. Biol., 7, 817-826.
24. Masuhara, M. et al. (1997) Cloning and characterization of novel CIS family genes. Biochem. Biophys. Res. Commun., 239, 439-446.
25. Matsumoto, A., Masuhara, M., Mitsui, K., Yokouchi, M., Ohtsubo, M., Misawa, H., Miyajima, A. and Yoshimura, A. (1997) CIS, a cytokine inducible SH2 protein, is a target of the JAK-STAT5 pathway and modulates STATS activation. Blood, 89, 3148-3154.
26. Meydan, N. et al. (1996) Inhibition of acute lymphoblastic leukaemia by a Jak-2 inhibitor. Nature, 379, 645-648.
27. Minamoto, S. et al. (1997) Cloning and functional analysis of new members of STAT induced STAT inhibitor (SSI) family: SSI-2 and SSI-3. Biochem. Biophys. Res. Commun., 237, 79-83.
28. Naka, T. et al. (1997) Structure and function of a new STAT-induced STAT inhibitor. Nature, 387, 924-929.
29. O'Shea, J.J. (1997) Jaks, STATs, cytokine signal transduction and immunoregulation: are we there yet? Immunity, 7, 1-11.
30. Plas, D.R., Johnson, R., Pingel, J.T., Matthews, R.J., Dalton, M., Roy, G., Chan, A.C. and Thomas, M.L. (1996) Direct regulation of ZAP-70 by SHP-1 in T-cell antigen receptor signaling. Science, 272, 1173-1176.
31. Russo, A.A., Jeffrey, P.D., Patten, A.K., Massague, J. and Pavletich, N.P. (1996) Crystal structure of the p27Kip1 cyclin-dependent-kinase inhibitor bound to the cyclin A-Cdk2 complex. Nature, 382, 325-331.
32. Russo, A.A., Tong, L., Lee, J., Jeffrey, P.D. and Pavletich, N.P. (1998) Structural basis for inhibition of the cyclin-dependent kinase Cdk6 by the tumour suppressor p16INK4a. Nature, 395, 237-243.
33. Sakamoto, H. et al. (1998) A Janus kinase inhibitor, JAB, is an interferon-γ inducible gene and confers resistance to interferons. Blood. 92, 1668-1676.
34. Scott, J.D., Fischer, E.H., Demaille, J.G. and Krebs, E.G. (1985) Identification of an inhibitory region of the heat-stable protein inhibitor of the cAMP-dependent protein kinase. Proc. Natl Acad. Sci. USA, 82, 4379-4383.
35. Shultz, L.D., Schweitzer, P.A., Rajan, T.V., Yi, T., Ihle, J.N., Matthews, R.J., Thomas, M.L. and Beier, D.R. (1993) Mutations at the murine motheaten locus are within the hematopoietic cell protein-tyrosine phosphatase (Hcph) gene. Cell, 73, 1445-1454.
36. Starr, R. et al. (1997) A family of cytokine-inducible inhibitors of signalling. Nature, 387, 917-921.
37. Weiss, A. and Schlessinger, J. (1998) Switching signals on or off by receptor dimerization. Cell, 94, 277-280.
38. Yoshimura, A., Ohkubo, T., Kiguchi, T., Jenkins, N.A., Gilbert, D.J., Copeland, N.G., Hara, T. and Miyajima, A. (1995) A novel cytokine-inducible gene CIS encodes an SH2-containing protein that binds to tyrosine-phosphorylated interleukin 3 and erythropoietin receptors. EMBO J., 14, 2816-2826.
39. Zhou, Y.J., Hanson, E.P., Chen, Y.Q., Magnuson, K., Chen, M., Swann, P.G., Wange, R.L., Changelian, P.S. and O'Shea, J.J. (1997) Distinct tyrosine phosphorylation sites in JAK3 kinase domain positively and negatively regulate its enzymatic activity. Proc. Natl Acad. Sci. USA, 94, 13850-13855.