메뉴 건너뛰기




Volumn 466, Issue , 2015, Pages 1-11

JAK2 activation by growth hormone and other cytokines

Author keywords

Class I cytokine receptors; Cytokine receptor signalling; Growth hormone; Growth hormone receptor; Janus kinase 2 (JAK2); Srk family kinases

Indexed keywords

BINDING PROTEIN; CYTOKINE RECEPTOR; GROWTH HORMONE; HOMODIMER; JANUS KINASE 2; RECEPTOR SUBUNIT; STAT PROTEIN; CYTOKINE; GROWTH HORMONE RECEPTOR; JAK2 PROTEIN, HUMAN; PROTEIN BINDING;

EID: 84922335259     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20141293     Document Type: Review
Times cited : (110)

References (118)
  • 1
    • 84896489589 scopus 로고    scopus 로고
    • Inhibition of IL-6 family cytokines by SOCS3
    • CrossRef PubMed
    • Babon, J. J., Varghese, L. N. and Nicola, N. A. (2014) Inhibition of IL-6 family cytokines by SOCS3. Semin. Immunol. 26, 13-19 CrossRef PubMed
    • (2014) Semin. Immunol. , vol.26 , pp. 13-19
    • Babon, J.J.1    Varghese, L.N.2    Nicola, N.A.3
  • 2
    • 33846903838 scopus 로고    scopus 로고
    • Cytokine receptor signaling through the Jak-Stat-Socs pathway in disease
    • CrossRef PubMed
    • O'Sullivan, L. A., Liongue, C., Lewis, R. S., Stephenson, S. E. and Ward, A. C. (2007) Cytokine receptor signaling through the Jak-Stat-Socs pathway in disease. Mol. Immunol. 44, 2497-2506 CrossRef PubMed
    • (2007) Mol. Immunol. , vol.44 , pp. 2497-2506
    • O'Sullivan, L.A.1    Liongue, C.2    Lewis, R.S.3    Stephenson, S.E.4    Ward, A.C.5
  • 5
    • 78649741783 scopus 로고    scopus 로고
    • GP130 at the nexus of inflammation, autoimmunity, and cancer
    • CrossRef
    • Silver, J. S. and Hunter, C. A. (2010) gp130 at the nexus of inflammation, autoimmunity, and cancer. J. Leukocyte Biol. 88, 1145-1156 CrossRef
    • (2010) J. Leukocyte Biol. , vol.88 , pp. 1145-1156
    • Silver, J.S.1    Hunter, C.A.2
  • 6
    • 84875277794 scopus 로고    scopus 로고
    • Lymphoid malignancies: Another face to the Janus kinases
    • CrossRef PubMed
    • Scott, L. M. (2013) Lymphoid malignancies: Another face to the Janus kinases. Blood Rev. 27, 63-70 CrossRef PubMed
    • (2013) Blood Rev. , vol.27 , pp. 63-70
    • Scott, L.M.1
  • 8
    • 81055147508 scopus 로고    scopus 로고
    • Prolactin regulation of the prostate gland: A female player in a male game
    • CrossRef PubMed
    • Goffin, V., Hoang, D. T., Bogorad, R. L. and Nevalainen, M. T. (2011) Prolactin regulation of the prostate gland: a female player in a male game. Nat. Rev. Urol. 8, 597-607CrossRef PubMed
    • (2011) Nat. Rev. Urol. , vol.8 , pp. 597-607
    • Goffin, V.1    Hoang, D.T.2    Bogorad, R.L.3    Nevalainen, M.T.4
  • 9
    • 2342445635 scopus 로고    scopus 로고
    • The JAK/STAT signaling pathway
    • CrossRef PubMed
    • Rawlings, J. S., Rosler, K. M. and Harrison, D. A. (2004) The JAK/STAT signaling pathway. J. Cell Sci. 117, 1281-1283 CrossRef PubMed
    • (2004) J. Cell Sci. , vol.117 , pp. 1281-1283
    • Rawlings, J.S.1    Rosler, K.M.2    Harrison, D.A.3
  • 10
    • 77955921088 scopus 로고    scopus 로고
    • The growth hormone receptor: Mechanism of activation and clinical implications
    • CrossRef PubMed
    • Brooks, A. J. and Waters, M. J. (2010) The growth hormone receptor: mechanism of activation and clinical implications. Nat. Rev. Endocrinol. 6, 515-525 CrossRef PubMed
    • (2010) Nat. Rev. Endocrinol. , vol.6 , pp. 515-525
    • Brooks, A.J.1    Waters, M.J.2
  • 11
    • 0025162844 scopus 로고
    • Structural design and molecular evolution of a cytokine receptor superfamily
    • CrossRef PubMed
    • Bazan, J. F. (1990) Structural design and molecular evolution of a cytokine receptor superfamily. Proc. Natl. Acad. Sci. U.S.A. 87, 6934-6938 CrossRef PubMed
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 6934-6938
    • Bazan, J.F.1
  • 12
    • 84902077833 scopus 로고    scopus 로고
    • Who climbs the tryptophan ladder? On the structure and function of the WSXWS motif in cytokine receptors and thrombospondin repeats
    • CrossRef
    • Olsen, J. G. and Kragelund, B. B. (2014) Who climbs the tryptophan ladder? On the structure and function of the WSXWS motif in cytokine receptors and thrombospondin repeats. Cytokine Growth Fact. Rev. 25, 337-341 CrossRef
    • (2014) Cytokine Growth Fact. Rev. , vol.25 , pp. 337-341
    • Olsen, J.G.1    Kragelund, B.B.2
  • 13
    • 34548329392 scopus 로고    scopus 로고
    • Evolution of class I cytokine receptors
    • CrossRef PubMed
    • Liongue, C. and Ward, A. C. (2007) Evolution of Class I cytokine receptors. BMC Evol. Biol. 7, 120 CrossRef PubMed
    • (2007) BMC Evol. Biol. , vol.7 , pp. 120
    • Liongue, C.1    Ward, A.C.2
  • 14
    • 0026598960 scopus 로고
    • Human growth hormone and extracellular domain of its receptor: Crystal structure of the complex
    • CrossRef PubMed
    • de Vos, A. M., Ultsch, M. and Kossiakoff, A. A. (1992) Human growth hormone and extracellular domain of its receptor: crystal structure of the complex. Science 255, 306-312 CrossRef PubMed
    • (1992) Science , vol.255 , pp. 306-312
    • De Vos, A.M.1    Ultsch, M.2    Kossiakoff, A.A.3
  • 17
    • 0026332810 scopus 로고
    • Dimerization of the extracellular domain of the human growth hormone receptor by a single hormone molecule
    • CrossRef PubMed
    • Cunningham, B. C., Ultsch, M., De Vos, A. M., Mulkerrin, M. G., Clauser, K. R. and Wells, J. A. (1991) Dimerization of the extracellular domain of the human growth hormone receptor by a single hormone molecule. Science 254, 821-825CrossRef PubMed
    • (1991) Science , vol.254 , pp. 821-825
    • Cunningham, B.C.1    Ultsch, M.2    De Vos, A.M.3    Mulkerrin, M.G.4    Clauser, K.R.5    Wells, J.A.6
  • 18
    • 78049441033 scopus 로고    scopus 로고
    • Structural characterization of the stem-stem dimerization interface between prolactin receptor chains complexed with the natural hormone
    • CrossRef PubMed
    • van Agthoven, J., Zhang, C., Tallet, E., Raynal, B., Hoos, S., Baron, B., England, P., Goffin, V. and Broutin, I. (2010) Structural characterization of the stem-stem dimerization interface between prolactin receptor chains complexed with the natural hormone. J. Mol. Biol. 404, 112-126 CrossRef PubMed
    • (2010) J. Mol. Biol. , vol.404 , pp. 112-126
    • Van Agthoven, J.1    Zhang, C.2    Tallet, E.3    Raynal, B.4    Hoos, S.5    Baron, B.6    England, P.7    Goffin, V.8    Broutin, I.9
  • 19
    • 0032188942 scopus 로고    scopus 로고
    • Efficiency of signalling through cytokine receptors depends critically on receptor orientation
    • CrossRef PubMed
    • Syed, R. S., Reid, S. W., Li, C., Cheetham, J. C., Aoki, K. H., Liu, B., Zhan, H., Osslund, T. D., Chirino, A. J., Zhang, J. et al. (1998) Efficiency of signalling through cytokine receptors depends critically on receptor orientation. Nature 395, 511-516CrossRef PubMed
    • (1998) Nature , vol.395 , pp. 511-516
    • Syed, R.S.1    Reid, S.W.2    Li, C.3    Cheetham, J.C.4    Aoki, K.H.5    Liu, B.6    Zhan, H.7    Osslund, T.D.8    Chirino, A.J.9    Zhang, J.10
  • 20
    • 0029819554 scopus 로고    scopus 로고
    • A sequential dimerization mechanism for erythropoietin receptor activation
    • CrossRef PubMed
    • Matthews, D. J., Topping, R. S., Cass, R. T. and Giebel, L. B. (1996) A sequential dimerization mechanism for erythropoietin receptor activation. Proc. Natl. Acad. Sci. U.S.A. 93, 9471-9476 CrossRef PubMed
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 9471-9476
    • Matthews, D.J.1    Topping, R.S.2    Cass, R.T.3    Giebel, L.B.4
  • 21
    • 0031057518 scopus 로고    scopus 로고
    • The role of receptor dimerization domain residues in growth hormone signaling
    • CrossRef PubMed
    • Chen, C., Brinkworth, R. and Waters, M. J. (1997) The role of receptor dimerization domain residues in growth hormone signaling. J. Biol. Chem. 272, 5133-5140CrossRef PubMed
    • (1997) J. Biol. Chem. , vol.272 , pp. 5133-5140
    • Chen, C.1    Brinkworth, R.2    Waters, M.J.3
  • 22
    • 0028966148 scopus 로고
    • Control of growth hormone (GH) binding protein release from human hepatoma cells expressing full-length GH receptor
    • PubMed
    • Harrison, S. M., Barnard, R., Ho, K. Y., Rajkovic, I. and Waters, M. J. (1995) Control of growth hormone (GH) binding protein release from human hepatoma cells expressing full-length GH receptor. Endocrinology 136, 651-659 PubMed
    • (1995) Endocrinology , vol.136 , pp. 651-659
    • Harrison, S.M.1    Barnard, R.2    Ho, K.Y.3    Rajkovic, I.4    Waters, M.J.5
  • 23
    • 0028097219 scopus 로고
    • Interaction of the growth hormone receptor cytoplasmic domain with the JAK2 tyrosine kinase
    • PubMed
    • Frank, S. J., Gilliland, G., Kraft, A. S. and Arnold, C. S. (1994) Interaction of the growth hormone receptor cytoplasmic domain with the JAK2 tyrosine kinase. Endocrinology 135, 2228-2239 PubMed
    • (1994) Endocrinology , vol.135 , pp. 2228-2239
    • Frank, S.J.1    Gilliland, G.2    Kraft, A.S.3    Arnold, C.S.4
  • 24
    • 0029980986 scopus 로고    scopus 로고
    • The box1 domain of the erythropoietin receptor specifies Janus kinase 2 activation and functions mitogenically within an interleukin 2 beta-receptor chimera
    • CrossRef PubMed
    • Jiang, N., He, T. C., Miyajima, A. and Wojchowski, D. M. (1996) The box1 domain of the erythropoietin receptor specifies Janus kinase 2 activation and functions mitogenically within an interleukin 2 beta-receptor chimera. J. Biol. Chem. 271, 16472-16476CrossRef PubMed
    • (1996) J. Biol. Chem. , vol.271 , pp. 16472-16476
    • Jiang, N.1    He, T.C.2    Miyajima, A.3    Wojchowski, D.M.4
  • 25
    • 15844389026 scopus 로고    scopus 로고
    • JAK2 is essential for activation of c-fos and c-myc promoters and cell proliferation through the human granulocyte-macrophage colony-stimulating factor receptor in BA/F3 cells
    • CrossRef PubMed
    • Watanabe, S., Itoh, T. and Arai, K. (1996) JAK2 is essential for activation of c-fos and c-myc promoters and cell proliferation through the human granulocyte-macrophage colony-stimulating factor receptor in BA/F3 cells. J. Biol. Chem. 271, 12681-12686CrossRef PubMed
    • (1996) J. Biol. Chem. , vol.271 , pp. 12681-12686
    • Watanabe, S.1    Itoh, T.2    Arai, K.3
  • 26
    • 33750971445 scopus 로고    scopus 로고
    • Two domains of the erythropoietin receptor are sufficient for JAK2 binding/activation and function
    • CrossRef PubMed
    • Pelletier, S., Gingras, S., Funakoshi-Tago, M., Howell, S. and Ihle, J. N. (2006) Two domains of the erythropoietin receptor are sufficient for Jak2 binding/activation and function. Mol. Cell. Biol. 26, 8527-8538 CrossRef PubMed
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 8527-8538
    • Pelletier, S.1    Gingras, S.2    Funakoshi-Tago, M.3    Howell, S.4    Ihle, J.N.5
  • 27
    • 0028956974 scopus 로고
    • Proline-rich sequence-mediated JAK2 association to the prolactin receptor is required but not sufficient for signal transduction
    • CrossRef PubMed
    • Lebrun, J. J., Ali, S., Ullrich, A. and Kelly, P. A. (1995) Proline-rich sequence-mediated Jak2 association to the prolactin receptor is required but not sufficient for signal transduction. J. Biol. Chem. 270, 10664-10670 CrossRef PubMed
    • (1995) J. Biol. Chem. , vol.270 , pp. 10664-10670
    • Lebrun, J.J.1    Ali, S.2    Ullrich, A.3    Kelly, P.A.4
  • 30
    • 0038609651 scopus 로고    scopus 로고
    • Hexameric structure and assembly of the interleukin-6/IL-6 alpha-receptor/gp130 complex
    • CrossRef PubMed
    • Boulanger, M. J., Chow, D. C., Brevnova, E. E. and Garcia, K. C. (2003) Hexameric structure and assembly of the interleukin-6/IL-6 alpha-receptor/gp130 complex. Science 300, 2101-2104 CrossRef PubMed
    • (2003) Science , vol.300 , pp. 2101-2104
    • Boulanger, M.J.1    Chow, D.C.2    Brevnova, E.E.3    Garcia, K.C.4
  • 31
    • 22444442637 scopus 로고    scopus 로고
    • Signaling conformations of the tall cytokine receptor gp130 when in complex with IL-6 and IL-6 receptor
    • CrossRef PubMed
    • Skiniotis, G., Boulanger, M. J., Garcia, K. C. and Walz, T. (2005) Signaling conformations of the tall cytokine receptor gp130 when in complex with IL-6 and IL-6 receptor. Nat. Struct. Mol. Biol. 12, 545-551 CrossRef PubMed
    • (2005) Nat. Struct. Mol. Biol. , vol.12 , pp. 545-551
    • Skiniotis, G.1    Boulanger, M.J.2    Garcia, K.C.3    Walz, T.4
  • 32
    • 34547866498 scopus 로고    scopus 로고
    • An unusual cytokine:IG-domain interaction revealed in the crystal structure of leukemia inhibitory factor (LIF) in complex with the LIF receptor
    • CrossRef PubMed
    • Huyton, T., Zhang, J. G., Luo, C. S., Lou, M. Z., Hilton, D. J., Nicola, N. A. and Garrett, T. P. (2007) An unusual cytokine:Ig-domain interaction revealed in the crystal structure of leukemia inhibitory factor (LIF) in complex with the LIF receptor. Proc. Natl. Acad. Sci. U.S.A. 104, 12737-12742 CrossRef PubMed
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 12737-12742
    • Huyton, T.1    Zhang, J.G.2    Luo, C.S.3    Lou, M.Z.4    Hilton, D.J.5    Nicola, N.A.6    Garrett, T.P.7
  • 33
    • 50249158577 scopus 로고    scopus 로고
    • Structural organization of a full-length gp130/LIF-R cytokine receptor transmembrane complex
    • CrossRef PubMed
    • Skiniotis, G., Lupardus, P. J., Martick, M., Walz, T. and Garcia, K. C. (2008) Structural organization of a full-length gp130/LIF-R cytokine receptor transmembrane complex. Mol. Cell 31, 737-748 CrossRef PubMed
    • (2008) Mol. Cell , vol.31 , pp. 737-748
    • Skiniotis, G.1    Lupardus, P.J.2    Martick, M.3    Walz, T.4    Garcia, K.C.5
  • 34
    • 0031738669 scopus 로고    scopus 로고
    • General classes and functions of four-helix bundle cytokines
    • CrossRef PubMed
    • Nicola, N. A. and Hilton, D. J. (1998) General classes and functions of four-helix bundle cytokines. Adv. Protein Chem. 52, 1-65 CrossRef PubMed
    • (1998) Adv. Protein Chem. , vol.52 , pp. 1-65
    • Nicola, N.A.1    Hilton, D.J.2
  • 35
    • 0030050701 scopus 로고    scopus 로고
    • Binding in the growth hormone receptor complex
    • CrossRef PubMed
    • Wells, J. A. (1996) Binding in the growth hormone receptor complex. Proc. Natl. Acad. Sci. U.S.A. 93, 1-6 CrossRef PubMed
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 1-6
    • Wells, J.A.1
  • 36
    • 0026764441 scopus 로고
    • Rational design of potent antagonists to the human growth hormone receptor
    • CrossRef PubMed
    • Fuh, G., Cunningham, B. C., Fukunaga, R., Nagata, S., Goeddel, D. V. and Wells, J. A. (1992) Rational design of potent antagonists to the human growth hormone receptor. Science 256, 1677-1680 CrossRef PubMed
    • (1992) Science , vol.256 , pp. 1677-1680
    • Fuh, G.1    Cunningham, B.C.2    Fukunaga, R.3    Nagata, S.4    Goeddel, D.V.5    Wells, J.A.6
  • 38
    • 0032570710 scopus 로고    scopus 로고
    • Activation of chimeric and full-length growth hormone receptors by growth hormone receptor monoclonal antibodies. A specific conformational change may be required for full-length receptor signaling
    • CrossRef PubMed
    • Rowlinson, S. W., Behncken, S. N., Rowland, J. E., Clarkson, R. W., Strasburger, C. J., Wu, Z., Baumbach, W. and Waters, M. J. (1998) Activation of chimeric and full-length growth hormone receptors by growth hormone receptor monoclonal antibodies. A specific conformational change may be required for full-length receptor signaling. J. Biol. Chem. 273, 5307-5314 CrossRef PubMed
    • (1998) J. Biol. Chem. , vol.273 , pp. 5307-5314
    • Rowlinson, S.W.1    Behncken, S.N.2    Rowland, J.E.3    Clarkson, R.W.4    Strasburger, C.J.5    Wu, Z.6    Baumbach, W.7    Waters, M.J.8
  • 39
    • 0242330190 scopus 로고    scopus 로고
    • Epitope map for a growth hormone receptor agonist monoclonal antibody, MAb 263
    • CrossRef PubMed
    • Wan, Y., Zheng, Y. Z., Harris, J. M., Brown, R. and Waters, M. J. (2003) Epitope map for a growth hormone receptor agonist monoclonal antibody, MAb 263. Mol. Endocrinol. 17, 2240-2250 CrossRef PubMed
    • (2003) Mol. Endocrinol. , vol.17 , pp. 2240-2250
    • Wan, Y.1    Zheng, Y.Z.2    Harris, J.M.3    Brown, R.4    Waters, M.J.5
  • 40
    • 0035040522 scopus 로고    scopus 로고
    • Binding and functional studies with the growth hormone receptor antagonist, B2036-PEG (pegvisomant), reveal effects of pegylation and evidence that it binds to a receptor dimer
    • PubMed
    • Ross, R. J., Leung, K. C., Maamra, M., Bennett, W., Doyle, N., Waters, M. J. and Ho, K. K. (2001) Binding and functional studies with the growth hormone receptor antagonist, B2036-PEG (pegvisomant), reveal effects of pegylation and evidence that it binds to a receptor dimer. J. Clin. Endocrinol. Metab. 86, 1716-1723 PubMed
    • (2001) J. Clin. Endocrinol. Metab. , vol.86 , pp. 1716-1723
    • Ross, R.J.1    Leung, K.C.2    Maamra, M.3    Bennett, W.4    Doyle, N.5    Waters, M.J.6    Ho, K.K.7
  • 41
    • 0035836645 scopus 로고    scopus 로고
    • Ligand-independent oligomerization of cell-surface erythropoietin receptor is mediated by the transmembrane domain
    • CrossRef PubMed
    • Constantinescu, S. N., Keren, T., Socolovsky, M., Nam, H., Henis, Y. I. and Lodish, H. F. (2001) Ligand-independent oligomerization of cell-surface erythropoietin receptor is mediated by the transmembrane domain. Proc. Natl. Acad. Sci. U.S.A. 98, 4379-4384CrossRef PubMed
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 4379-4384
    • Constantinescu, S.N.1    Keren, T.2    Socolovsky, M.3    Nam, H.4    Henis, Y.I.5    Lodish, H.F.6
  • 43
    • 0030575833 scopus 로고    scopus 로고
    • Dimerisation of the glycophorin A transmembrane segment in membranes probed with the ToxR transcription activator
    • CrossRef PubMed
    • Langosch, D., Brosig, B., Kolmar, H. and Fritz, H. J. (1996) Dimerisation of the glycophorin A transmembrane segment in membranes probed with the ToxR transcription activator. J. Mol. Biol. 263, 525-530 CrossRef PubMed
    • (1996) J. Mol. Biol. , vol.263 , pp. 525-530
    • Langosch, D.1    Brosig, B.2    Kolmar, H.3    Fritz, H.J.4
  • 46
    • 79953754929 scopus 로고    scopus 로고
    • Growth hormone signaling in human T47D breast cancer cells: Potential role for a growth hormone receptor-prolactin receptor complex
    • CrossRef PubMed
    • Xu, J., Zhang, Y., Berry, P. A., Jiang, J., Lobie, P. E., Langenheim, J. F., Chen, W. Y. and Frank, S. J. (2011) Growth hormone signaling in human T47D breast cancer cells: potential role for a growth hormone receptor-prolactin receptor complex. Mol. Endocrinol. 25, 597-610 CrossRef PubMed
    • (2011) Mol. Endocrinol. , vol.25 , pp. 597-610
    • Xu, J.1    Zhang, Y.2    Berry, P.A.3    Jiang, J.4    Lobie, P.E.5    Langenheim, J.F.6    Chen, W.Y.7    Frank, S.J.8
  • 47
    • 0033548259 scopus 로고    scopus 로고
    • Crystallographic evidence for preformed dimers of erythropoietin receptor before ligand activation
    • CrossRef PubMed
    • Livnah, O., Stura, E. A., Middleton, S. A., Johnson, D. L., Jolliffe, L. K. and Wilson, I. A. (1999) Crystallographic evidence for preformed dimers of erythropoietin receptor before ligand activation. Science 283, 987-990 CrossRef PubMed
    • (1999) Science , vol.283 , pp. 987-990
    • Livnah, O.1    Stura, E.A.2    Middleton, S.A.3    Johnson, D.L.4    Jolliffe, L.K.5    Wilson, I.A.6
  • 48
    • 0942276402 scopus 로고    scopus 로고
    • The interface between self-assembling erythropoietin receptor transmembrane segments corresponds to a membrane-spanning leucine zipper
    • CrossRef PubMed
    • Ruan, W., Becker, V., Klingmuller, U. and Langosch, D. (2004) The interface between self-assembling erythropoietin receptor transmembrane segments corresponds to a membrane-spanning leucine zipper. J. Biol. Chem. 279, 3273-3279 CrossRef PubMed
    • (2004) J. Biol. Chem. , vol.279 , pp. 3273-3279
    • Ruan, W.1    Becker, V.2    Klingmuller, U.3    Langosch, D.4
  • 49
    • 0038297325 scopus 로고    scopus 로고
    • Dimerization and signal transduction of the growth hormone receptor
    • CrossRef PubMed
    • Gent, J., Van Den Eijnden, M., Van Kerkhof, P. and Strous, G. J. (2003) Dimerization and signal transduction of the growth hormone receptor. Mol. Endocrinol. 17, 967-975CrossRef PubMed
    • (2003) Mol. Endocrinol. , vol.17 , pp. 967-975
    • Gent, J.1    Van Den Eijnden, M.2    Van Kerkhof, P.3    Strous, G.J.4
  • 51
    • 84922283196 scopus 로고    scopus 로고
    • A new mechanism for growth hormone receptor activation of JAK2, and implications for related cytokine receptors
    • CrossRef PubMed
    • Waters, M. J., Brooks, A. J. and Chhabra, Y. (2014) A new mechanism for growth hormone receptor activation of JAK2, and implications for related cytokine receptors. Jak-Stat. 3, e29569 CrossRef PubMed
    • (2014) Jak-stat. , vol.3 , pp. e29569
    • Waters, M.J.1    Brooks, A.J.2    Chhabra, Y.3
  • 52
    • 0034595858 scopus 로고    scopus 로고
    • Growth hormone (GH)-independent dimerization of GH receptor by a leucine zipper results in constitutive activation
    • CrossRef PubMed
    • Behncken, S. N., Billestrup, N., Brown, R., Amstrup, J., Conway-Campbell, B. and Waters, M. J. (2000) Growth hormone (GH)-independent dimerization of GH receptor by a leucine zipper results in constitutive activation. J. Biol. Chem. 275, 17000-17007CrossRef PubMed
    • (2000) J. Biol. Chem. , vol.275 , pp. 17000-17007
    • Behncken, S.N.1    Billestrup, N.2    Brown, R.3    Amstrup, J.4    Conway-Campbell, B.5    Waters, M.J.6
  • 53
    • 79955858161 scopus 로고    scopus 로고
    • Activation of GH signaling and GH-independent stimulation of growth in zebrafish by introduction of a constitutively activated GHR construct
    • CrossRef PubMed
    • Ahmed, A. S., Xiong, F., Pang, S. C., He, M. D., Waters, M. J., Zhu, Z. Y. and Sun, Y. H. (2011) Activation of GH signaling and GH-independent stimulation of growth in zebrafish by introduction of a constitutively activated GHR construct. Transgenic Res. 20, 557-567 CrossRef PubMed
    • (2011) Transgenic Res. , vol.20 , pp. 557-567
    • Ahmed, A.S.1    Xiong, F.2    Pang, S.C.3    He, M.D.4    Waters, M.J.5    Zhu, Z.Y.6    Sun, Y.H.7
  • 54
    • 0029804197 scopus 로고    scopus 로고
    • Functional replacement of cytokine receptor extracellular domains by leucine zippers
    • CrossRef PubMed
    • Patel, N., Herrman, J. M., Timans, J. C. and Kastelein, R. A. (1996) Functional replacement of cytokine receptor extracellular domains by leucine zippers. J. Biol. Chem. 271, 30386-30391 CrossRef PubMed
    • (1996) J. Biol. Chem. , vol.271 , pp. 30386-30391
    • Patel, N.1    Herrman, J.M.2    Timans, J.C.3    Kastelein, R.A.4
  • 55
    • 33745598848 scopus 로고    scopus 로고
    • Forced dimerization of gp130 leads to constitutive STAT3 activation, cytokine-independent growth, and blockade of differentiation of embryonic stem cells
    • CrossRef PubMed
    • Stuhlmann-Laeisz, C., Lang, S., Chalaris, A., Krzysztof, P., Enge, S., Eichler, J., Klingmuller, U., Samuel, M., Ernst, M., Rose-John, S. and Scheller, J. (2006) Forced dimerization of gp130 leads to constitutive STAT3 activation, cytokine-independent growth, and blockade of differentiation of embryonic stem cells. Mol. Biol. Cell 17, 2986-2995 CrossRef PubMed
    • (2006) Mol. Biol. Cell , vol.17 , pp. 2986-2995
    • Stuhlmann-Laeisz, C.1    Lang, S.2    Chalaris, A.3    Krzysztof, P.4    Enge, S.5    Eichler, J.6    Klingmuller, U.7    Samuel, M.8    Ernst, M.9    Rose-John, S.10    Scheller, J.11
  • 56
    • 0344413478 scopus 로고    scopus 로고
    • Active and inactive orientations of the transmembrane and cytosolic domains of the erythropoietin receptor dimer
    • CrossRef PubMed
    • Seubert, N., Royer, Y., Staerk, J., Kubatzky, K. F., Moucadel, V., Krishnakumar, S., Smith, S. O. and Constantinescu, S. N. (2003) Active and inactive orientations of the transmembrane and cytosolic domains of the erythropoietin receptor dimer. Mol. Cell 12, 1239-1250 CrossRef PubMed
    • (2003) Mol. Cell , vol.12 , pp. 1239-1250
    • Seubert, N.1    Royer, Y.2    Staerk, J.3    Kubatzky, K.F.4    Moucadel, V.5    Krishnakumar, S.6    Smith, S.O.7    Constantinescu, S.N.8
  • 58
    • 33344455687 scopus 로고    scopus 로고
    • An amphipathic motif at the transmembrane-cytoplasmic junction prevents autonomous activation of the thrombopoietin receptor
    • CrossRef PubMed
    • Staerk, J., Lacout, C., Sato, T., Smith, S. O., Vainchenker, W. and Constantinescu, S. N. (2006) An amphipathic motif at the transmembrane-cytoplasmic junction prevents autonomous activation of the thrombopoietin receptor. Blood 107, 1864-1871CrossRef PubMed
    • (2006) Blood , vol.107 , pp. 1864-1871
    • Staerk, J.1    Lacout, C.2    Sato, T.3    Smith, S.O.4    Vainchenker, W.5    Constantinescu, S.N.6
  • 61
    • 77951251864 scopus 로고    scopus 로고
    • Turning the growth hormone receptor on: Evidence that hormone binding induces subunit rotation
    • CrossRef PubMed
    • Poger, D. and Mark, A. E. (2010) Turning the growth hormone receptor on: evidence that hormone binding induces subunit rotation. Proteins 78, 1163-1174 CrossRef PubMed
    • (2010) Proteins , vol.78 , pp. 1163-1174
    • Poger, D.1    Mark, A.E.2
  • 62
    • 0032755252 scopus 로고    scopus 로고
    • Disulfide linkage of growth hormone (GH) receptors (GHR) reflects GH-induced GHR dimerization. Association of JAK2 with the GHR is enhanced by receptor dimerization
    • CrossRef PubMed
    • Zhang, Y., Jiang, J., Kopchick, J. J. and Frank, S. J. (1999) Disulfide linkage of growth hormone (GH) receptors (GHR) reflects GH-induced GHR dimerization. Association of JAK2 with the GHR is enhanced by receptor dimerization. J. Biol. Chem. 274, 33072-33084 CrossRef PubMed
    • (1999) J. Biol. Chem. , vol.274 , pp. 33072-33084
    • Zhang, Y.1    Jiang, J.2    Kopchick, J.J.3    Frank, S.J.4
  • 63
    • 0038371050 scopus 로고    scopus 로고
    • Autoinhibition of JAK2 tyrosine kinase is dependent on specific regions in its pseudokinase domain
    • CrossRef PubMed
    • Saharinen, P., Vihinen, M. and Silvennoinen, O. (2003) Autoinhibition of Jak2 tyrosine kinase is dependent on specific regions in its pseudokinase domain. Mol. Biol. Cell 14, 1448-1459 CrossRef PubMed
    • (2003) Mol. Biol. Cell , vol.14 , pp. 1448-1459
    • Saharinen, P.1    Vihinen, M.2    Silvennoinen, O.3
  • 64
    • 77953482860 scopus 로고    scopus 로고
    • Perspectives for the use of structural information and chemical genetics to develop inhibitors of Janus kinases
    • PubMed
    • Haan, C., Behrmann, I. and Haan, S. (2010) Perspectives for the use of structural information and chemical genetics to develop inhibitors of Janus kinases. J. Cell. Mol. Med. 14, 504-527 PubMed
    • (2010) J. Cell. Mol. Med. , vol.14 , pp. 504-527
    • Haan, C.1    Behrmann, I.2    Haan, S.3
  • 65
    • 41949118675 scopus 로고    scopus 로고
    • Dimerization by a cytokine receptor is necessary for constitutive activation of JAK2V617F
    • CrossRef PubMed
    • Lu, X., Huang, L. J. and Lodish, H. F. (2008) Dimerization by a cytokine receptor is necessary for constitutive activation of JAK2V617F. J. Biol. Chem. 283, 5258-5266CrossRef PubMed
    • (2008) J. Biol. Chem. , vol.283 , pp. 5258-5266
    • Lu, X.1    Huang, L.J.2    Lodish, H.F.3
  • 66
    • 30044437118 scopus 로고    scopus 로고
    • Expression of a homodimeric type I cytokine receptor is required for JAK2V617F-mediated transformation
    • CrossRef PubMed
    • Lu, X., Levine, R., Tong, W., Wernig, G., Pikman, Y., Zarnegar, S., Gilliland, D. G. and Lodish, H. (2005) Expression of a homodimeric type I cytokine receptor is required for JAK2V617F-mediated transformation. Proc. Natl. Acad. Sci. U.S.A. 102, 18962-18967CrossRef PubMed
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 18962-18967
    • Lu, X.1    Levine, R.2    Tong, W.3    Wernig, G.4    Pikman, Y.5    Zarnegar, S.6    Gilliland, D.G.7    Lodish, H.8
  • 67
    • 40749093314 scopus 로고    scopus 로고
    • Jak2FERM domain interaction with the erythropoietin receptor regulates Jak2 kinase activity
    • CrossRef PubMed
    • Funakoshi-Tago, M., Pelletier, S., Moritake, H., Parganas, E. and Ihle, J. N. (2008) Jak2FERM domain interaction with the erythropoietin receptor regulates Jak2 kinase activity. Mol. Cell. Biol. 28, 1792-1801 CrossRef PubMed
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 1792-1801
    • Funakoshi-Tago, M.1    Pelletier, S.2    Moritake, H.3    Parganas, E.4    Ihle, J.N.5
  • 68
    • 84894272750 scopus 로고    scopus 로고
    • Mechanistic insights into activation and SOCS3-mediated inhibition of myeloproliferative neoplasm-associated JAK2 mutants from biochemical and structural analyses
    • CrossRef PubMed
    • Varghese, L. N., Ungureanu, D., Liau, N. P., Young, S. N., Laktyushin, A., Hammaren, H., Lucet, I. S., Nicola, N. A., Silvennoinen, O., Babon, J. J. and Murphy, J. M. (2014)Mechanistic insights into activation and SOCS3-mediated inhibition of myeloproliferative neoplasm-associated JAK2 mutants from biochemical and structural analyses. Biochem. J. 458, 395-405 CrossRef PubMed
    • (2014) Biochem. J. , vol.458 , pp. 395-405
    • Varghese, L.N.1    Ungureanu, D.2    Liau, N.P.3    Young, S.N.4    Laktyushin, A.5    Hammaren, H.6    Lucet, I.S.7    Nicola, N.A.8    Silvennoinen, O.9    Babon, J.J.10    Murphy, J.M.11
  • 70
    • 84904638434 scopus 로고    scopus 로고
    • The molecular regulation of Janus kinase (JAK) activation
    • CrossRef PubMed
    • Babon, J. J., Lucet, I. S., Murphy, J. M., Nicola, N. A. and Varghese, L. N. (2014) The molecular regulation of Janus kinase (JAK) activation. Biochem. J. 462, 1-13CrossRef PubMed
    • (2014) Biochem. J. , vol.462 , pp. 1-13
    • Babon, J.J.1    Lucet, I.S.2    Murphy, J.M.3    Nicola, N.A.4    Varghese, L.N.5
  • 71
    • 84901840527 scopus 로고    scopus 로고
    • Structure of the pseudokinase-kinase domains from protein kinase TYK2 reveals a mechanism for Janus kinase (JAK) autoinhibition
    • CrossRef PubMed
    • Lupardus, P. J., Ultsch, M., Wallweber, H., Bir Kohli, P., Johnson, A. R. and Eigenbrot, C. (2014) Structure of the pseudokinase-kinase domains from protein kinase TYK2 reveals a mechanism for Janus kinase (JAK) autoinhibition. Proc. Natl. Acad. Sci. U.S.A. 111, 8025-8030 CrossRef PubMed
    • (2014) Proc. Natl. Acad. Sci. U.S.A. , vol.111 , pp. 8025-8030
    • Lupardus, P.J.1    Ultsch, M.2    Wallweber, H.3    Bir Kohli, P.4    Johnson, A.R.5    Eigenbrot, C.6
  • 75
    • 0035045092 scopus 로고    scopus 로고
    • Prediction of the structure of human Janus kinase 2 (JAK2) comprising the two carboxy-terminal domains reveals a mechanism for autoregulation
    • CrossRef PubMed
    • Lindauer, K., Loerting, T., Liedl, K. R. and Kroemer, R. T. (2001) Prediction of the structure of human Janus kinase 2 (JAK2) comprising the two carboxy-terminal domains reveals a mechanism for autoregulation. Protein Eng. 14, 27-37 CrossRef PubMed
    • (2001) Protein Eng. , vol.14 , pp. 27-37
    • Lindauer, K.1    Loerting, T.2    Liedl, K.R.3    Kroemer, R.T.4
  • 76
    • 84870009088 scopus 로고    scopus 로고
    • Regulation of JAK2 activation by Janus homology 2: Evidence from molecular dynamics simulations
    • CrossRef
    • Wan, S. and Coveney, P. V. (2012) Regulation of JAK2 activation by Janus homology 2: evidence from molecular dynamics simulations. J. Chem. Inform. Mod. 52, 2992-3000 CrossRef
    • (2012) J. Chem. Inform. Mod. , vol.52 , pp. 2992-3000
    • Wan, S.1    Coveney, P.V.2
  • 77
    • 84876910676 scopus 로고    scopus 로고
    • Ab initio modeling and experimental assessment of Janus Kinase 2 (JAK2) kinase-pseudokinase complex structure
    • CrossRef PubMed
    • Wan, X., Ma, Y., McClendon, C. L., Huang, L. J. and Huang, N. (2013) Ab initio modeling and experimental assessment of Janus Kinase 2 (JAK2) kinase-pseudokinase complex structure. PLoS Comput. Biol. 9, e1003022 CrossRef PubMed
    • (2013) PLoS Comput. Biol. , vol.9 , pp. e1003022
    • Wan, X.1    Ma, Y.2    McClendon, C.L.3    Huang, L.J.4    Huang, N.5
  • 78
    • 78651254183 scopus 로고    scopus 로고
    • Structural snapshots of full-length Jak1, a transmembrane gp130/IL-6/IL-6Ralpha cytokine receptor complex, and the receptor-Jak1 holocomplex
    • CrossRef PubMed
    • Lupardus, P. J., Skiniotis, G., Rice, A. J., Thomas, C., Fischer, S., Walz, T. and Garcia, K. C. (2011) Structural snapshots of full-length Jak1, a transmembrane gp130/IL-6/IL-6Ralpha cytokine receptor complex, and the receptor-Jak1 holocomplex. Structure 19, 45-55 CrossRef PubMed
    • (2011) Structure , vol.19 , pp. 45-55
    • Lupardus, P.J.1    Skiniotis, G.2    Rice, A.J.3    Thomas, C.4    Fischer, S.5    Walz, T.6    Garcia, K.C.7
  • 79
    • 34548240698 scopus 로고    scopus 로고
    • Role of JAK2 in the pathogenesis and therapy of myeloproliferative disorders
    • CrossRef PubMed
    • Levine, R. L., Pardanani, A., Tefferi, A. and Gilliland, D. G. (2007) Role of JAK2 in the pathogenesis and therapy of myeloproliferative disorders. Nat. Rev. Cancer 7, 673-683CrossRef PubMed
    • (2007) Nat. Rev. Cancer , vol.7 , pp. 673-683
    • Levine, R.L.1    Pardanani, A.2    Tefferi, A.3    Gilliland, D.G.4
  • 84
    • 84897556667 scopus 로고    scopus 로고
    • Improved targeting of JAK2 leads to increased therapeutic efficacy in myeloproliferative neoplasms
    • CrossRef PubMed
    • Bhagwat, N., Koppikar, P., Keller, M., Marubayashi, S., Shank, K., Rampal, R., Qi, J., Kleppe, M., Patel, H. J., Shah, S. K. et al. (2014) Improved targeting of JAK2 leads to increased therapeutic efficacy in myeloproliferative neoplasms. Blood 123, 2075-2083CrossRef PubMed
    • (2014) Blood , vol.123 , pp. 2075-2083
    • Bhagwat, N.1    Koppikar, P.2    Keller, M.3    Marubayashi, S.4    Shank, K.5    Rampal, R.6    Qi, J.7    Kleppe, M.8    Patel, H.J.9    Shah, S.K.10
  • 85
    • 84900859210 scopus 로고    scopus 로고
    • The role of pacritinib in the management of myelofibrosis
    • CrossRef PubMed
    • Duong, V. H. and Komrokji, R. S. (2014) The role of pacritinib in the management of myelofibrosis. Expert Rev. Hematol. 7, 325-332 CrossRef PubMed
    • (2014) Expert Rev. Hematol. , vol.7 , pp. 325-332
    • Duong, V.H.1    Komrokji, R.S.2
  • 86
    • 84922337086 scopus 로고    scopus 로고
    • Profile of pacritinib and its potential in the treatment of hematologic disorders
    • CrossRef PubMed
    • Hatzimichael, E., Tsolas, E. and Briasoulis, E. (2014) Profile of pacritinib and its potential in the treatment of hematologic disorders. J. Blood Med. 5, 143-152 CrossRef PubMed
    • (2014) J. Blood Med. , vol.5 , pp. 143-152
    • Hatzimichael, E.1    Tsolas, E.2    Briasoulis, E.3
  • 87
    • 84889596004 scopus 로고    scopus 로고
    • Open-label study of oral CEP-701 (lestaurtinib) in patients with polycythaemia vera or essential thrombocythaemia with JAK2-V617F mutation
    • CrossRef
    • Hexner, E., Roboz, G., Hoffman, R., Luger, S., Mascarenhas, J., Carroll, M., Clementi, R., Bensen-Kennedy, D. and Moliterno, A. (2014) Open-label study of oral CEP-701 (lestaurtinib) in patients with polycythaemia vera or essential thrombocythaemia with JAK2-V617F mutation. Brit. J. Haematol. 164, 83-93 CrossRef
    • (2014) Brit. J. Haematol. , vol.164 , pp. 83-93
    • Hexner, E.1    Roboz, G.2    Hoffman, R.3    Luger, S.4    Mascarenhas, J.5    Carroll, M.6    Clementi, R.7    Bensen-Kennedy, D.8    Moliterno, A.9
  • 90
    • 33751526473 scopus 로고    scopus 로고
    • Ligand-independent dimerization of the human prolactin receptor isoforms: Functional implications
    • CrossRef PubMed
    • Gadd, S. L. and Clevenger, C. V. (2006) Ligand-independent dimerization of the human prolactin receptor isoforms: functional implications. Mol. Endocrinol. 20, 2734-2746CrossRef PubMed
    • (2006) Mol. Endocrinol. , vol.20 , pp. 2734-2746
    • Gadd, S.L.1    Clevenger, C.V.2
  • 93
    • 77954368725 scopus 로고    scopus 로고
    • Crystal structure of the entire ectodomain of gp130: Insights into the molecular assembly of the tall cytokine receptor complexes
    • CrossRef PubMed
    • Xu, Y., Kershaw, N. J., Luo, C. S., Soo, P., Pocock, M. J., Czabotar, P. E., Hilton, D. J., Nicola, N. A., Garrett, T. P. and Zhang, J. G. (2010) Crystal structure of the entire ectodomain of gp130: insights into the molecular assembly of the tall cytokine receptor complexes. J. Biol. Chem. 285, 21214-21218 CrossRef PubMed
    • (2010) J. Biol. Chem. , vol.285 , pp. 21214-21218
    • Xu, Y.1    Kershaw, N.J.2    Luo, C.S.3    Soo, P.4    Pocock, M.J.5    Czabotar, P.E.6    Hilton, D.J.7    Nicola, N.A.8    Garrett, T.P.9    Zhang, J.G.10
  • 94
    • 0029991793 scopus 로고    scopus 로고
    • Differential activation of acute phase response factor/Stat3 and Stat1 via the cytoplasmic domain of the interleukin 6 signal transducer gp130. II. Src homology SH2 domains define the specificity of stat factor activation
    • CrossRef PubMed
    • Hemmann, U., Gerhartz, C., Heesel, B., Sasse, J., Kurapkat, G., Grotzinger, J., Wollmer, A., Zhong, Z., Darnell, Jr JE, Graeve, L. et al. (1996) Differential activation of acute phase response factor/Stat3 and Stat1 via the cytoplasmic domain of the interleukin 6 signal transducer gp130. II. Src homology SH2 domains define the specificity of stat factor activation. J. Biol. Chem. 271, 12999-13007 CrossRef PubMed
    • (1996) J. Biol. Chem. , vol.271 , pp. 12999-13007
    • Hemmann, U.1    Gerhartz, C.2    Heesel, B.3    Sasse, J.4    Kurapkat, G.5    Grotzinger, J.6    Wollmer, A.7    Zhong, Z.8    Darnell, J.E.9    Graeve, L.10
  • 95
    • 0027473576 scopus 로고
    • Signal transduction mediated by growth hormone receptor and its chimeric molecules with the granulocyte colony-stimulating factor receptor
    • CrossRef PubMed
    • Ishizaka-Ikeda, E., Fukunaga, R., Wood, W. I., Goeddel, D. V. and Nagata, S. (1993)Signal transduction mediated by growth hormone receptor and its chimeric molecules with the granulocyte colony-stimulating factor receptor. Proc. Natl. Acad. Sci. U.S.A. 90, 123-127 CrossRef PubMed
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 123-127
    • Ishizaka-Ikeda, E.1    Fukunaga, R.2    Wood, W.I.3    Goeddel, D.V.4    Nagata, S.5
  • 96
    • 34347216041 scopus 로고    scopus 로고
    • Role of the growth hormone (GH) receptor transmembrane domain in receptor predimerization and GH-induced activation
    • CrossRef PubMed
    • Yang, N., Wang, X., Jiang, J. and Frank, S. J. (2007) Role of the growth hormone (GH) receptor transmembrane domain in receptor predimerization and GH-induced activation. Mol. Endocrinol. 21, 1642-1655 CrossRef PubMed
    • (2007) Mol. Endocrinol. , vol.21 , pp. 1642-1655
    • Yang, N.1    Wang, X.2    Jiang, J.3    Frank, S.J.4
  • 97
    • 0037026594 scopus 로고    scopus 로고
    • An activating mutation in the transmembrane domain of the granulocyte colony-stimulating factor receptor in patients with acute myeloid leukemia
    • CrossRef PubMed
    • Forbes, L. V., Gale, R. E., Pizzey, A., Pouwels, K., Nathwani, A. and Linch, D. C. (2002)An activating mutation in the transmembrane domain of the granulocyte colony-stimulating factor receptor in patients with acute myeloid leukemia. Oncogene 21, 5981-5989 CrossRef PubMed
    • (2002) Oncogene , vol.21 , pp. 5981-5989
    • Forbes, L.V.1    Gale, R.E.2    Pizzey, A.3    Pouwels, K.4    Nathwani, A.5    Linch, D.C.6
  • 99
    • 84904704303 scopus 로고    scopus 로고
    • Granulocyte colony-stimulating factor receptor mutations in myeloid malignancy
    • CrossRef PubMed
    • Liongue, C. and Ward, A. C. (2014) Granulocyte colony-stimulating factor receptor mutations in myeloid malignancy. Front. Oncol. 4, 93 CrossRef PubMed
    • (2014) Front. Oncol. , vol.4 , pp. 93
    • Liongue, C.1    Ward, A.C.2
  • 100
    • 70350452280 scopus 로고    scopus 로고
    • The Asn505 mutation of the c-MPL gene, which causes familial essential thrombocythemia, induces autonomous homodimerization of the c-Mpl protein due to strong amino acid polarity
    • CrossRef PubMed
    • Ding, J., Komatsu, H., Iida, S., Yano, H., Kusumoto, S., Inagaki, A., Mori, F., Ri, M., Ito, A., Wakita, A. et al. (2009) The Asn505 mutation of the c-MPL gene, which causes familial essential thrombocythemia, induces autonomous homodimerization of the c-Mpl protein due to strong amino acid polarity. Blood 114, 3325-3328 CrossRef PubMed
    • (2009) Blood , vol.114 , pp. 3325-3328
    • Ding, J.1    Komatsu, H.2    Iida, S.3    Yano, H.4    Kusumoto, S.5    Inagaki, A.6    Mori, F.7    Ri, M.8    Ito, A.9    Wakita, A.10
  • 101
    • 80051814548 scopus 로고    scopus 로고
    • Effects of clinically relevant MPL mutations in the transmembrane domain revealed at the atomic level through computational modeling
    • CrossRef PubMed
    • Lee, T. S., Kantarjian, H., Ma, W., Yeh, C. H., Giles, F. and Albitar, M. (2011) Effects of clinically relevant MPL mutations in the transmembrane domain revealed at the atomic level through computational modeling. PLoS ONE 6, e23396 CrossRef PubMed
    • (2011) PLoS ONE , vol.6 , pp. e23396
    • Lee, T.S.1    Kantarjian, H.2    Ma, W.3    Yeh, C.H.4    Giles, F.5    Albitar, M.6
  • 102
    • 79960190017 scopus 로고    scopus 로고
    • Thrombopoietin receptor activation: Transmembrane helix dimerization, rotation, and allosteric modulation
    • CrossRef PubMed
    • Matthews, E. E., Thevenin, D., Rogers, J. M., Gotow, L., Lira, P. D., Reiter, L. A., Brissette, W. H. and Engelman, D. M. (2011) Thrombopoietin receptor activation: transmembrane helix dimerization, rotation, and allosteric modulation. FASEB J. 25, 2234-2244 CrossRef PubMed
    • (2011) FASEB J. , vol.25 , pp. 2234-2244
    • Matthews, E.E.1    Thevenin, D.2    Rogers, J.M.3    Gotow, L.4    Lira, P.D.5    Reiter, L.A.6    Brissette, W.H.7    Engelman, D.M.8
  • 103
    • 66749134179 scopus 로고    scopus 로고
    • The influence of domain structures on the signal transduction of chimeric receptors derived from the erythropoietin receptor
    • CrossRef PubMed
    • Liu, W., Kawahara, M., Ueda, H. and Nagamune, T. (2009) The influence of domain structures on the signal transduction of chimeric receptors derived from the erythropoietin receptor. J. Biochem. 145, 575-584 CrossRef PubMed
    • (2009) J. Biochem. , vol.145 , pp. 575-584
    • Liu, W.1    Kawahara, M.2    Ueda, H.3    Nagamune, T.4
  • 105
    • 48249130514 scopus 로고    scopus 로고
    • JAK2, but not Src family kinases, is required for STAT, ERK, and Akt signaling in response to growth hormone in preadipocytes and hepatoma cells
    • CrossRef PubMed
    • Jin, H., Lanning, N. J. and Carter-Su, C. (2008) JAK2, but not Src family kinases, is required for STAT, ERK, and Akt signaling in response to growth hormone in preadipocytes and hepatoma cells. Mol. Endocrinol. 22, 1825-1841CrossRef PubMed
    • (2008) Mol. Endocrinol. , vol.22 , pp. 1825-1841
    • Jin, H.1    Lanning, N.J.2    Carter-Su, C.3
  • 108
    • 0032525115 scopus 로고    scopus 로고
    • Lyn physically associates with the erythropoietin receptor and may play a role in activation of the Stat5 pathway
    • PubMed
    • Chin, H., Arai, A., Wakao, H., Kamiyama, R., Miyasaka, N. and Miura, O. (1998) Lyn physically associates with the erythropoietin receptor and may play a role in activation of the Stat5 pathway. Blood 91, 3734-3745 PubMed
    • (1998) Blood , vol.91 , pp. 3734-3745
    • Chin, H.1    Arai, A.2    Wakao, H.3    Kamiyama, R.4    Miyasaka, N.5    Miura, O.6
  • 109
    • 84898612227 scopus 로고    scopus 로고
    • Lyn kinase plays important roles in erythroid expansion, maturation and erythropoietin receptor signalling by regulating inhibitory signalling pathways that control survival
    • CrossRef PubMed
    • Slavova-Azmanova, N. S., Kucera, N., Louw, A., Satiaputra, J., Handoko, A., Singer, P., Stone, L., McCarthy, D. J., Klinken, S. P., Hibbs, M. L. and Ingley, E. (2014) Lyn kinase plays important roles in erythroid expansion, maturation and erythropoietin receptor signalling by regulating inhibitory signalling pathways that control survival. Biochem. J. 459, 455-466 CrossRef PubMed
    • (2014) Biochem. J. , vol.459 , pp. 455-466
    • Slavova-Azmanova, N.S.1    Kucera, N.2    Louw, A.3    Satiaputra, J.4    Handoko, A.5    Singer, P.6    Stone, L.7    McCarthy, D.J.8    Klinken, S.P.9    Hibbs, M.L.10    Ingley, E.11
  • 110
    • 0031456720 scopus 로고    scopus 로고
    • Signal transduction of interleukin-6 involves tyrosine phosphorylation of multiple cytosolic proteins and activation of Src-family kinases Fyn, Hck, and Lyn in multiple myeloma cell lines
    • PubMed
    • Hallek, M., Neumann, C., Schaffer, M., Danhauser-Riedl, S., von Bubnoff, N., de Vos, G., Druker, B. J., Yasukawa, K., Griffin, J. D. and Emmerich, B. (1997) Signal transduction of interleukin-6 involves tyrosine phosphorylation of multiple cytosolic proteins and activation of Src-family kinases Fyn, Hck, and Lyn in multiple myeloma cell lines. Exp. Hematol. 25, 1367-1377 PubMed
    • (1997) Exp. Hematol. , vol.25 , pp. 1367-1377
    • Hallek, M.1    Neumann, C.2    Schaffer, M.3    Danhauser-Riedl, S.4    Von Bubnoff, N.5    De Vos, G.6    Druker, B.J.7    Yasukawa, K.8    Griffin, J.D.9    Emmerich, B.10
  • 111
    • 0033996525 scopus 로고    scopus 로고
    • Association of Lyn tyrosine kinase to the GM-CSF and IL-3 receptor common betac subunit and role of Src tyrosine kinases in DNA synthesis and anti-apoptosis
    • CrossRef
    • Dahl, M. E., Arai, K. I. and Watanabe, S. (2000) Association of Lyn tyrosine kinase to the GM-CSF and IL-3 receptor common betac subunit and role of Src tyrosine kinases in DNA synthesis and anti-apoptosis. Genes Cells Dev. Mol. Cell. Mech. 5, 143-153 CrossRef
    • (2000) Genes Cells Dev. Mol. Cell. Mech. , vol.5 , pp. 143-153
    • Dahl, M.E.1    Arai, K.I.2    Watanabe, S.3
  • 112
    • 0033083258 scopus 로고    scopus 로고
    • The mapping of the Lyn kinase binding site of the common beta subunit of IL-3/granulocyte-macrophage colony-stimulating factor/IL-5 receptor
    • PubMed
    • Adachi, T., Pazdrak, K., Stafford, S. and Alam, R. (1999) The mapping of the Lyn kinase binding site of the common beta subunit of IL-3/granulocyte-macrophage colony-stimulating factor/IL-5 receptor. J. Immunol. 162, 1496-1501 PubMed
    • (1999) J. Immunol. , vol.162 , pp. 1496-1501
    • Adachi, T.1    Pazdrak, K.2    Stafford, S.3    Alam, R.4
  • 114
    • 33750606752 scopus 로고    scopus 로고
    • The duplicitous nature of the Lyn tyrosine kinase in growth factor signaling
    • CrossRef PubMed
    • Hibbs, M. L. and Harder, K. W. (2006) The duplicitous nature of the Lyn tyrosine kinase in growth factor signaling. Growth Factors (Chur, Switzerland). 24, 137-149CrossRef PubMed
    • (2006) Growth Factors (Chur, Switzerland) , vol.24 , pp. 137-149
    • Hibbs, M.L.1    Harder, K.W.2
  • 115
    • 79960800539 scopus 로고    scopus 로고
    • Mutations in the transmembrane and juxtamembrane domains enhance IL27R transforming activity
    • CrossRef PubMed
    • Lambert, Q. T., Pradhan, A., Roll, J. D. and Reuther, G. W. (2011) Mutations in the transmembrane and juxtamembrane domains enhance IL27R transforming activity. Biochem. J. 438, 155-164 CrossRef PubMed
    • (2011) Biochem. J. , vol.438 , pp. 155-164
    • Lambert, Q.T.1    Pradhan, A.2    Roll, J.D.3    Reuther, G.W.4
  • 116
    • 33646381647 scopus 로고    scopus 로고
    • Active conformation of the erythropoietin receptor: Random and cysteine-scanning mutagenesis of the extracellular juxtamembrane and transmembrane domains
    • CrossRef PubMed
    • Lu, X., Gross, A. W. and Lodish, H. F. (2006) Active conformation of the erythropoietin receptor: random and cysteine-scanning mutagenesis of the extracellular juxtamembrane and transmembrane domains. J. Biol. Chem. 281, 7002-7011 CrossRef PubMed
    • (2006) J. Biol. Chem. , vol.281 , pp. 7002-7011
    • Lu, X.1    Gross, A.W.2    Lodish, H.F.3
  • 117
    • 77951499323 scopus 로고    scopus 로고
    • F104S c-Mpl responds to a transmembrane domain-binding thrombopoietin receptor agonist: Proof of concept that selected receptor mutations in congenital amegakaryocytic thrombocytopenia can be stimulated with alternative thrombopoietic agents
    • CrossRef PubMed
    • Fox, N. E., Lim, J., Chen, R. and Geddis, A. E. (2010) F104S c-Mpl responds to a transmembrane domain-binding thrombopoietin receptor agonist: proof of concept that selected receptor mutations in congenital amegakaryocytic thrombocytopenia can be stimulated with alternative thrombopoietic agents. Exp. Hematol. 38, 384-391CrossRef PubMed
    • (2010) Exp. Hematol. , vol.38 , pp. 384-391
    • Fox, N.E.1    Lim, J.2    Chen, R.3    Geddis, A.E.4
  • 118
    • 77649247830 scopus 로고    scopus 로고
    • Construction and genetic selection of small transmembrane proteins that activate the human erythropoietin receptor
    • CrossRef PubMed
    • Cammett, T. J., Jun, S. J., Cohen, E. B., Barrera, F. N., Engelman, D. M. and Dimaio, D. (2010) Construction and genetic selection of small transmembrane proteins that activate the human erythropoietin receptor. Proc. Natl. Acad. Sci. U.S.A. 107, 3447-3452 CrossRef PubMed
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 3447-3452
    • Cammett, T.J.1    Jun, S.J.2    Cohen, E.B.3    Barrera, F.N.4    Engelman, D.M.5    Dimaio, D.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.