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Volumn 344, Issue 6185, 2014, Pages

Mechanism of activation of protein kinase JAK2 by the growth hormone receptor

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE; GROWTH HORMONE RECEPTOR; JANUS KINASE 2; LEUCINE ZIPPER PROTEIN; PROTEIN KINASE; PSEUDOKINASE; UNCLASSIFIED DRUG; JAK2 PROTEIN, HUMAN;

EID: 84900432315     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.1249783     Document Type: Article
Times cited : (333)

References (55)
  • 1
    • 77955921088 scopus 로고    scopus 로고
    • The growth hormone receptor: Mechanism of activation and clinical implications
    • doi: 10.1038/nrendo.2010.123; pmid: 20664532
    • A. J. Brooks, M. J. Waters, The growth hormone receptor: Mechanism of activation and clinical implications. Nat. Rev. Endocrinol. 6, 515-525 (2010). doi: 10.1038/nrendo.2010.123; pmid: 20664532
    • (2010) Nat. Rev. Endocrinol. , vol.6 , pp. 515-525
    • Brooks, A.J.1    Waters, M.J.2
  • 2
    • 0026598960 scopus 로고
    • Human growth hormone and extracellular domain of its receptor: Crystal structure of the complex
    • doi: 10.1126/science.1549776; pmid: 1549776
    • A. M. de Vos, M. Ultsch, A. A. Kossiakoff, Human growth hormone and extracellular domain of its receptor: Crystal structure of the complex. Science 255, 306-312 (1992). doi: 10.1126/science.1549776; pmid: 1549776
    • (1992) Science , vol.255 , pp. 306-312
    • De Vos, A.M.1    Ultsch, M.2    Kossiakoff, A.A.3
  • 3
    • 0026332810 scopus 로고
    • Dimerization of the extracellular domain of the human growth hormone receptor by a single hormone molecule
    • doi: 10.1126/science.1948064; pmid: 1948064
    • B. C. Cunningham et al., Dimerization of the extracellular domain of the human growth hormone receptor by a single hormone molecule. Science 254, 821-825 (1991). doi: 10.1126/science.1948064; pmid: 1948064
    • (1991) Science , vol.254 , pp. 821-825
    • Cunningham, B.C.1
  • 4
    • 0026764441 scopus 로고
    • Rational design of potent antagonists to the human growth hormone receptor
    • doi: 10.1126/science.256.5064.1677; pmid: 1535167
    • G. Fuh et al., Rational design of potent antagonists to the human growth hormone receptor. Science 256, 1677-1680 (1992). doi: 10.1126/science.256.5064. 1677; pmid: 1535167
    • (1992) Science , vol.256 , pp. 1677-1680
    • Fuh, G.1
  • 5
    • 0030050701 scopus 로고    scopus 로고
    • Binding in the growth hormone receptor complex
    • doi: 10.1073/pnas.93.1.1; pmid: 8552582
    • J. A. Wells, Binding in the growth hormone receptor complex. Proc. Natl. Acad. Sci. U.S.A. 93, 1-6 (1996). doi: 10.1073/pnas.93.1.1; pmid: 8552582
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 1-6
    • Wells, J.A.1
  • 6
    • 0037162458 scopus 로고    scopus 로고
    • Ligand-independent growth hormone receptor dimerization occurs in the endoplasmic reticulum and is required for ubiquitin system-dependent endocytosis
    • doi: 10.1073/pnas.152294299; pmid: 12105275
    • J. Gent, P. van Kerkhof, M. Roza, G. Bu, G. J. Strous, Ligand-independent growth hormone receptor dimerization occurs in the endoplasmic reticulum and is required for ubiquitin system-dependent endocytosis. Proc. Natl. Acad. Sci. U.S.A. 99, 9858-9863 (2002). doi: 10.1073/pnas.152294299; pmid: 12105275
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 9858-9863
    • Gent, J.1    Van Kerkhof, P.2    Roza, M.3    Bu, G.4    Strous, G.J.5
  • 7
    • 26944493862 scopus 로고    scopus 로고
    • Model for growth hormone receptor activation based on subunit rotation within a receptor dimer
    • doi: 10.1038/nsmb977; pmid: 16116438
    • R. J. Brown et al., Model for growth hormone receptor activation based on subunit rotation within a receptor dimer. Nat. Struct. Mol. Biol. 12, 814-821 (2005). doi: 10.1038/nsmb977; pmid: 16116438
    • (2005) Nat. Struct. Mol. Biol. , vol.12 , pp. 814-821
    • Brown, R.J.1
  • 8
    • 0035936596 scopus 로고    scopus 로고
    • Self assembly of the transmembrane domain promotes signal transduction through the erythropoietin receptor
    • doi: 10.1016/S0960-9822(01)00018-5; pmid: 11231127
    • K. F. Kubatzky et al., Self assembly of the transmembrane domain promotes signal transduction through the erythropoietin receptor. Curr. Biol. 11, 110-115 (2001). doi: 10.1016/S0960-9822(01)00018-5; pmid: 11231127
    • (2001) Curr. Biol. , vol.11 , pp. 110-115
    • Kubatzky, K.F.1
  • 9
    • 33751526473 scopus 로고    scopus 로고
    • Ligand-independent dimerization of the human prolactin receptor isoforms: Functional implications
    • doi: 10.1210/me.2006-0114; pmid: 16840534
    • S. L. Gadd, C. V. Clevenger, Ligand-independent dimerization of the human prolactin receptor isoforms: Functional implications. Mol. Endocrinol. 20, 2734-2746 (2006). doi: 10.1210/me.2006-0114; pmid: 16840534
    • (2006) Mol. Endocrinol. , vol.20 , pp. 2734-2746
    • Gadd, S.L.1    Clevenger, C.V.2
  • 10
    • 79960190017 scopus 로고    scopus 로고
    • Thrombopoietin receptor activation: Transmembrane helix dimerization, rotation, and allosteric modulation
    • doi: 10.1096/fj.10-178673; pmid: 21402716
    • E. E. Matthews et al., Thrombopoietin receptor activation: Transmembrane helix dimerization, rotation, and allosteric modulation. FASEB J. 25, 2234-2244 (2011). doi: 10.1096/fj.10-178673; pmid: 21402716
    • (2011) FASEB J. , vol.25 , pp. 2234-2244
    • Matthews, E.E.1
  • 11
    • 0031766635 scopus 로고    scopus 로고
    • An antagonist peptide-EPO receptor complex suggests that receptor dimerization is not sufficient for activation
    • doi: 10.1038/2965; pmid: 9808045
    • O. Livnah et al., An antagonist peptide-EPO receptor complex suggests that receptor dimerization is not sufficient for activation. Nat. Struct. Biol. 5, 993-1004 (1998). doi: 10.1038/2965; pmid: 9808045
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 993-1004
    • Livnah, O.1
  • 12
    • 78651254183 scopus 로고    scopus 로고
    • Structural snapshots of full-length Jak1, a transmembrane gp130/IL-6/IL-6Rα cytokine receptor complex, and the receptor-Jak1 holocomplex
    • doi: 10.1016/j.str.2010.10.010; pmid: 21220115
    • P. J. Lupardus et al., Structural snapshots of full-length Jak1, a transmembrane gp130/IL-6/IL-6Rα cytokine receptor complex, and the receptor-Jak1 holocomplex. Structure 19, 45-55 (2011). doi: 10.1016/j.str.2010. 10.010; pmid: 21220115
    • (2011) Structure , vol.19 , pp. 45-55
    • Lupardus, P.J.1
  • 13
    • 84900411836 scopus 로고    scopus 로고
    • Single-letter abbreviations for the amino acid residues are as follows: A, Ala; C, Cys; D, Asp; E, Glu; F, Phe; G, Gly; H, His; I, Ile; K, Lys; L, Leu; M, Met; N, Asn; P, Pro; Q, Gln; R, Arg; S, Ser; T, Thr; V, Val; W, Trp; and Y, Tyr
    • Single-letter abbreviations for the amino acid residues are as follows: A, Ala; C, Cys; D, Asp; E, Glu; F, Phe; G, Gly; H, His; I, Ile; K, Lys; L, Leu; M, Met; N, Asn; P, Pro; Q, Gln; R, Arg; S, Ser; T, Thr; V, Val; W, Trp; and Y, Tyr.
  • 14
    • 40749093314 scopus 로고    scopus 로고
    • Jak2 FERM domain interaction with the erythropoietin receptor regulates Jak2 kinase activity
    • doi: 10.1128/MCB.01447-07; pmid: 18160720
    • M. Funakoshi-Tago, S. Pelletier, H. Moritake, E. Parganas, J. N. Ihle, Jak2 FERM domain interaction with the erythropoietin receptor regulates Jak2 kinase activity. Mol. Cell. Biol. 28, 1792-1801 (2008). doi: 10.1128/MCB.01447-07; pmid: 18160720
    • (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
  • 15
    • 41949118675 scopus 로고    scopus 로고
    • Dimerization by a cytokine receptor is necessary for constitutive activation of JAK2V617F
    • doi: 10.1074/jbc.M707125200; pmid: 18158285
    • X. Lu, L. J. Huang, H. F. Lodish, Dimerization by a cytokine receptor is necessary for constitutive activation of JAK2V617F. J. Biol. Chem. 283, 5258-5266 (2008). doi: 10.1074/jbc.M707125200; pmid: 18158285
    • (2008) J. Biol. Chem. , vol.283 , pp. 5258-5266
    • Lu, X.1    Huang, L.J.2    Lodish, H.F.3
  • 16
    • 0242267061 scopus 로고    scopus 로고
    • Janus kinase 2 determinants for growth hormone receptor association, surface assembly, and signaling
    • doi: 10.1210/me.2003-0256; pmid: 12920237
    • K. He et al., Janus kinase 2 determinants for growth hormone receptor association, surface assembly, and signaling. Mol. Endocrinol. 17, 2211-2227 (2003). doi: 10.1210/me.2003-0256; pmid: 12920237
    • (2003) Mol. Endocrinol. , vol.17 , pp. 2211-2227
    • He, K.1
  • 17
    • 0030575833 scopus 로고    scopus 로고
    • Dimerisation of the glycophorin A transmembrane segment in membranes probed with the ToxR transcription activator
    • doi: 10.1006/jmbi.1996.0595; pmid: 8918935
    • D. Langosch, B. Brosig, H. Kolmar, H. J. Fritz, Dimerisation of the glycophorin A transmembrane segment in membranes probed with the ToxR transcription activator. J. Mol. Biol. 263, 525-530 (1996). doi: 10.1006/jmbi.1996.0595; pmid: 8918935
    • (1996) J. Mol. Biol. , vol.263 , pp. 525-530
    • Langosch, D.1    Brosig, B.2    Kolmar, H.3    Fritz, H.J.4
  • 18
    • 0942276402 scopus 로고    scopus 로고
    • The interface between self-assembling erythropoietin receptor transmembrane segments corresponds to a membrane-spanning leucine zipper
    • doi: 10.1074/jbc.M309311200; pmid: 14602718
    • W. Ruan, V. Becker, U. Klingmüller, D. Langosch, The interface between self-assembling erythropoietin receptor transmembrane segments corresponds to a membrane-spanning leucine zipper. J. Biol. Chem. 279, 3273-3279 (2004). doi: 10.1074/jbc.M309311200; pmid: 14602718
    • (2004) J. Biol. Chem. , vol.279 , pp. 3273-3279
    • Ruan, W.1    Becker, V.2    Klingmüller, U.3    Langosch, D.4
  • 19
    • 0035836645 scopus 로고    scopus 로고
    • Ligand-independent oligomerization of cell-surface erythropoietin receptor is mediated by the transmembrane domain
    • doi: 10.1073/pnas.081069198; pmid: 11296286
    • S. N. Constantinescu et al., Ligand-independent oligomerization of cell-surface erythropoietin receptor is mediated by the transmembrane domain. Proc. Natl. Acad. Sci. U.S.A. 98, 4379-4384 (2001). doi: 10.1073/pnas.081069198; pmid: 11296286
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 4379-4384
    • Constantinescu, S.N.1
  • 20
    • 79951971437 scopus 로고    scopus 로고
    • Homo-FRET imaging as a tool to quantify protein and lipid clustering
    • doi: 10.1002/cphc.201000801; pmid: 21344588
    • A. N. Bader et al., Homo-FRET imaging as a tool to quantify protein and lipid clustering. ChemPhysChem 12, 475-483 (2011). doi: 10.1002/cphc.201000801; pmid: 21344588
    • (2011) ChemPhysChem , vol.12 , pp. 475-483
    • Bader, A.N.1
  • 21
    • 84856471945 scopus 로고    scopus 로고
    • Dynamic imaging of homo-FRET in live cells by fluorescence anisotropy microscopy
    • doi: 10.1016/B978-0-12-388448-0.00024-3; pmid: 22289460
    • S. Ghosh, S. Saha, D. Goswami, S. Bilgrami, S. Mayor, Dynamic imaging of homo-FRET in live cells by fluorescence anisotropy microscopy. Methods Enzymol. 505, 291-327 (2012). doi: 10.1016/B978-0-12-388448-0.00024-3; pmid: 22289460
    • (2012) Methods Enzymol. , vol.505 , pp. 291-327
    • Ghosh, S.1    Saha, S.2    Goswami, D.3    Bilgrami, S.4    Mayor, S.5
  • 22
    • 79551711208 scopus 로고    scopus 로고
    • Full characterization of GPCR monomer-dimer dynamic equilibrium by single molecule imaging
    • doi: 10.1083/jcb.201009128; pmid: 21300851
    • R. S. Kasai et al., Full characterization of GPCR monomer-dimer dynamic equilibrium by single molecule imaging. J. Cell Biol. 192, 463-480 (2011). doi: 10.1083/jcb.201009128; pmid: 21300851
    • (2011) J. Cell Biol. , vol.192 , pp. 463-480
    • Kasai, R.S.1
  • 23
    • 18744408187 scopus 로고    scopus 로고
    • Dimerization of receptor protein-tyrosine phosphatase alpha in living cells
    • doi: 10.1186/1471-2121-2-8; pmid: 11401727
    • L. G. J. Tertoolen et al., Dimerization of receptor protein-tyrosine phosphatase alpha in living cells. BMC Cell Biol. 2, 8 (2001). doi: 10.1186/1471-2121-2-8; pmid: 11401727
    • (2001) BMC Cell Biol. , vol.2 , pp. 8
    • Tertoolen, L.G.J.1
  • 24
    • 0033533817 scopus 로고    scopus 로고
    • Dimerization inhibits the activity of receptor-like protein-tyrosine phosphatase-alpha
    • doi: 10.1038/44170; pmid: 10524630
    • G. Jiang et al., Dimerization inhibits the activity of receptor-like protein-tyrosine phosphatase-alpha. Nature 401, 606-610 (1999). doi: 10.1038/44170; pmid: 10524630
    • (1999) Nature , vol.401 , pp. 606-610
    • Jiang, G.1
  • 25
    • 0033859771 scopus 로고    scopus 로고
    • Receptor-like protein tyrosine phosphatase a homodimerizes on the cell surface
    • doi: 10.1128/MCB.20.16.5917-5929.2000; pmid: 10913175
    • G. Jiang, J. den Hertog, T. Hunter, Receptor-like protein tyrosine phosphatase a homodimerizes on the cell surface. Mol. Cell. Biol. 20, 5917-5929 (2000). doi: 10.1128/MCB.20.16.5917-5929.2000; pmid: 10913175
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 5917-5929
    • Jiang, G.1    Den Hertog, J.2    Hunter, T.3
  • 26
    • 16444366687 scopus 로고    scopus 로고
    • Structural requirements of the extracellular to transmembrane domain junction for erythropoietin receptor function
    • doi: 10.1074/jbc.M411251200; pmid: 15657048
    • K. F. Kubatzky et al., Structural requirements of the extracellular to transmembrane domain junction for erythropoietin receptor function. J. Biol. Chem. 280, 14844-14854 (2005). doi: 10.1074/jbc.M411251200; pmid: 15657048
    • (2005) J. Biol. Chem. , vol.280 , pp. 14844-14854
    • Kubatzky, K.F.1
  • 27
    • 0037133698 scopus 로고    scopus 로고
    • Surface-exposed positions in the transmembrane helices of the lactose permease of Escherichia coli determined by intermolecular thiol cross-linking
    • doi: 10.1073/pnas.052703699; pmid: 11904412
    • L. Guan, F. D. Murphy, H. R. Kaback, Surface-exposed positions in the transmembrane helices of the lactose permease of Escherichia coli determined by intermolecular thiol cross-linking. Proc. Natl. Acad. Sci. U.S.A. 99, 3475-3480 (2002). doi: 10.1073/pnas.052703699; pmid: 11904412
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 3475-3480
    • Guan, L.1    Murphy, F.D.2    Kaback, H.R.3
  • 28
    • 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
    • doi: 10.1074/jbc.274.46.33072; pmid: 10551877
    • Y. Zhang, J. Jiang, J. J. Kopchick, S. J. Frank, 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 (1999). doi: 10.1074/jbc.274.46.33072; pmid: 10551877
    • (1999) J. Biol. Chem. , vol.274 , pp. 33072-33084
    • Zhang, Y.1    Jiang, J.2    Kopchick, J.J.3    Frank, S.J.4
  • 29
    • 0034595858 scopus 로고    scopus 로고
    • Growth hormone (GH)-independent dimerization of GH receptor by a leucine zipper results in constitutive activation
    • doi: 10.1074/jbc.275.22.17000; pmid: 10828073
    • S. N. Behncken et al., Growth hormone (GH)-independent dimerization of GH receptor by a leucine zipper results in constitutive activation. J. Biol. Chem. 275, 17000-17007 (2000). doi: 10.1074/jbc.275.22.17000; pmid: 10828073
    • (2000) J. Biol. Chem. , vol.275 , pp. 17000-17007
    • Behncken, S.N.1
  • 30
    • 34347222583 scopus 로고    scopus 로고
    • Design and implementation of bimolecular fluorescence complementation (BiFC) assays for the visualization of protein interactions in living cells
    • doi: 10.1038/nprot.2006.201; pmid: 17406412
    • T. K. Kerppola, Design and implementation of bimolecular fluorescence complementation (BiFC) assays for the visualization of protein interactions in living cells. Nat. Protoc. 1, 1278-1286 (2006). doi: 10.1038/nprot.2006.201; pmid: 17406412
    • (2006) Nat. Protoc. , vol.1 , pp. 1278-1286
    • Kerppola, T.K.1
  • 31
    • 0028294901 scopus 로고
    • A single amino acid substitution in the exoplasmic domain of the human growth hormone (GH) receptor confers familial GH resistance (Laron syndrome) with positive GH-binding activity by abolishing receptor homodimerization
    • pmid: 8137822
    • P. Duquesnoy et al., A single amino acid substitution in the exoplasmic domain of the human growth hormone (GH) receptor confers familial GH resistance (Laron syndrome) with positive GH-binding activity by abolishing receptor homodimerization. EMBO J. 13, 1386-1395 (1994). pmid: 8137822
    • (1994) EMBO J. , vol.13 , pp. 1386-1395
    • Duquesnoy, P.1
  • 32
    • 33748063281 scopus 로고    scopus 로고
    • Spatio-temporal kinetics of growth hormone receptor signaling in single cells using FRET microscopy
    • doi: 10.1016/j.ghir.2006.06.001; pmid: 16950496
    • E. Biener-Ramanujan, V. K. Ramanujan, B. Herman, A. Gertler, Spatio-temporal kinetics of growth hormone receptor signaling in single cells using FRET microscopy. Growth Horm. IGF Res. 16, 247-257 (2006). doi: 10.1016/j.ghir.2006.06.001; pmid: 16950496
    • (2006) Growth Horm. IGF Res. , vol.16 , pp. 247-257
    • Biener-Ramanujan, E.1    Ramanujan, V.K.2    Herman, B.3    Gertler, A.4
  • 33
    • 50249158577 scopus 로고    scopus 로고
    • Structural organization of a full-length gp130/LIF-R cytokine receptor transmembrane complex
    • doi: 10.1016/j.molcel.2008.08.011; pmid: 18775332
    • G. Skiniotis, P. J. Lupardus, M. Martick, T. Walz, K. C. Garcia, Structural organization of a full-length gp130/LIF-R cytokine receptor transmembrane complex. Mol. Cell 31, 737-748 (2008). doi: 10.1016/j.molcel.2008. 08.011; pmid: 18775332
    • (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
    • 33344455687 scopus 로고    scopus 로고
    • An amphipathic motif at the transmembrane-cytoplasmic junction prevents autonomous activation of the thrombopoietin receptor
    • doi: 10.1182/blood-2005-06-2600; pmid: 16249382
    • J. Staerk et al., An amphipathic motif at the transmembrane-cytoplasmic junction prevents autonomous activation of the thrombopoietin receptor. Blood 107, 1864-1871 (2006). doi: 10.1182/blood-2005-06-2600; pmid: 16249382
    • (2006) Blood , vol.107 , pp. 1864-1871
    • Staerk, J.1
  • 36
    • 49449113010 scopus 로고    scopus 로고
    • The MARTINI coarse-grained force field: Extension to proteins
    • doi: 10.1021/ct700324x
    • L. Monticelli et al., The MARTINI coarse-grained force field: Extension to proteins. J. Chem. Theory Comput. 4, 819-834 (2008). doi: 10.1021/ct700324x
    • (2008) J. Chem. Theory Comput. , vol.4 , pp. 819-834
    • Monticelli, L.1
  • 37
    • 77954354757 scopus 로고    scopus 로고
    • Lipid-modulated sequence-specific association of glycophorin A in membranes
    • doi: 10.1016/j.bpj.2010.04.005; pmid: 20655857
    • L. Janosi, A. Prakash, M. Doxastakis, Lipid-modulated sequence-specific association of glycophorin A in membranes. Biophys. J. 99, 284-292 (2010). doi: 10.1016/j.bpj.2010.04.005; pmid: 20655857
    • (2010) Biophys. J. , vol.99 , pp. 284-292
    • Janosi, L.1    Prakash, A.2    Doxastakis, M.3
  • 38
    • 20444499328 scopus 로고    scopus 로고
    • Insights into the recognition and association of transmembrane α-helices. The free energy of α-helix dimerization in glycophorin A
    • doi: 10.1021/ja050581y; pmid: 15941282
    • J. Hénin, A. Pohorille, C. Chipot, Insights into the recognition and association of transmembrane α-helices. The free energy of α-helix dimerization in glycophorin A. J. Am. Chem. Soc. 127, 8478-8484 (2005). doi: 10.1021/ja050581y; pmid: 15941282
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 8478-8484
    • Hénin, J.1    Pohorille, A.2    Chipot, C.3
  • 39
    • 80054687051 scopus 로고    scopus 로고
    • GxxxG motifs, phenylalanine, and cholesterol guide the self-association of transmembrane domains of ErbB2 receptors
    • doi: 10.1016/j.bpj.2011.09.017; pmid: 22004749
    • A. Prakash, L. Janosi, M. Doxastakis, GxxxG motifs, phenylalanine, and cholesterol guide the self-association of transmembrane domains of ErbB2 receptors. Biophys. J. 101, 1949-1958 (2011). doi: 10.1016/j.bpj.2011.09.017; pmid: 22004749
    • (2011) Biophys. J. , vol.101 , pp. 1949-1958
    • Prakash, A.1    Janosi, L.2    Doxastakis, M.3
  • 41
    • 77951251864 scopus 로고    scopus 로고
    • Turning the growth hormone receptor on: Evidence that hormone binding induces subunit rotation
    • doi: 10.1002/prot.22636; pmid: 19927328
    • D. Poger, A. E. Mark, Turning the growth hormone receptor on: Evidence that hormone binding induces subunit rotation. Proteins 78, 1163-1174 (2010). doi: 10.1002/prot.22636; pmid: 19927328
    • (2010) Proteins , vol.78 , pp. 1163-1174
    • Poger, D.1    Mark, A.E.2
  • 42
    • 0031057518 scopus 로고    scopus 로고
    • The role of receptor dimerization domain residues in growth hormone signaling
    • doi: 10.1074/jbc.272.8.5133; pmid: 9030580
    • C. Chen, R. Brinkworth, M. J. Waters, The role of receptor dimerization domain residues in growth hormone signaling. J. Biol. Chem. 272, 5133-5140 (1997). doi: 10.1074/jbc.272.8.5133; pmid: 9030580
    • (1997) J. Biol. Chem. , vol.272 , pp. 5133-5140
    • Chen, C.1    Brinkworth, R.2    Waters, M.J.3
  • 43
    • 0037417787 scopus 로고    scopus 로고
    • Determination of the energetics governing the regulatory step in growth hormone-induced receptor homodimerization
    • doi: 10.1073/pnas.0235023100; pmid: 12552121
    • B. Bernat, G. Pal, M. Sun, A. A. Kossiakoff, Determination of the energetics governing the regulatory step in growth hormone-induced receptor homodimerization. Proc. Natl. Acad. Sci. U.S.A. 100, 952-957 (2003). doi: 10.1073/pnas.0235023100; pmid: 12552121
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 952-957
    • Bernat, B.1    Pal, G.2    Sun, M.3    Kossiakoff, A.A.4
  • 44
    • 0036215093 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway regulates the availability of the GH receptor
    • doi: 10.1210/endo.143.4.8755; pmid: 11897680
    • P. van Kerkhof, M. Smeets, G. J. Strous, The ubiquitin-proteasome pathway regulates the availability of the GH receptor. Endocrinology 143, 1243-1252 (2002). doi: 10.1210/endo.143.4.8755; pmid: 11897680
    • (2002) Endocrinology , vol.143 , pp. 1243-1252
    • Van Kerkhof, P.1    Smeets, M.2    Strous, G.J.3
  • 45
    • 0027742729 scopus 로고
    • Interferon-induced nuclear signalling by Jak protein tyrosine kinases
    • doi: 10.1038/366583a0; pmid: 7504785
    • O. Silvennoinen, J. N. Ihle, J. Schlessinger, D. E. Levy, Interferon-induced nuclear signalling by Jak protein tyrosine kinases. Nature 366, 583-585 (1993). doi: 10.1038/366583a0; pmid: 7504785
    • (1993) Nature , vol.366 , pp. 583-585
    • Silvennoinen, O.1    Ihle, J.N.2    Schlessinger, J.3    Levy, D.E.4
  • 46
    • 30144436273 scopus 로고    scopus 로고
    • The structural basis of Janus kinase 2 inhibition by a potent and specific pan-Janus kinase inhibitor
    • doi: 10.1182/blood-2005-06-2413; pmid: 16174768
    • I. S. Lucet et al., The structural basis of Janus kinase 2 inhibition by a potent and specific pan-Janus kinase inhibitor. Blood 107, 176-183 (2006). doi: 10.1182/blood-2005-06-2413; pmid: 16174768
    • (2006) Blood , vol.107 , pp. 176-183
    • Lucet, I.S.1
  • 47
    • 84864668290 scopus 로고    scopus 로고
    • Crystal structures of the JAK2 pseudokinase domain and the pathogenic mutant V617F
    • doi: 10.1038/nsmb.2348; pmid: 22820988
    • R. M. Bandaranayake et al., Crystal structures of the JAK2 pseudokinase domain and the pathogenic mutant V617F. Nat. Struct. Mol. Biol. 19, 754-759 (2012). doi: 10.1038/nsmb.2348; pmid: 22820988
    • (2012) Nat. Struct. Mol. Biol. , vol.19 , pp. 754-759
    • Bandaranayake, R.M.1
  • 48
    • 33646381647 scopus 로고    scopus 로고
    • Active conformation of the erythropoietin receptor: Random and cysteine-scanning mutagenesis of the extracellular juxtamembrane and transmembrane domains
    • doi: 10.1074/jbc.M512638200; pmid: 16414957
    • X. Lu, A. W. Gross, H. F. Lodish, Active conformation of the erythropoietin receptor: Random and cysteine-scanning mutagenesis of the extracellular juxtamembrane and transmembrane domains. J. Biol. Chem. 281, 7002-7011 (2006). doi: 10.1074/jbc.M512638200; pmid: 16414957
    • (2006) J. Biol. Chem. , vol.281 , pp. 7002-7011
    • Lu, X.1    Gross, A.W.2    Lodish, H.F.3
  • 49
    • 0344413478 scopus 로고    scopus 로고
    • Active and inactive orientations of the transmembrane and cytosolic domains of the erythropoietin receptor dimer
    • doi: 10.1016/S1097-2765(03)00389-7; pmid: 14636581
    • N. Seubert et al., Active and inactive orientations of the transmembrane and cytosolic domains of the erythropoietin receptor dimer. Mol. Cell 12, 1239-1250 (2003). doi: 10.1016/S1097-2765(03)00389-7; pmid: 14636581
    • (2003) Mol. Cell , vol.12 , pp. 1239-1250
    • Seubert, N.1
  • 50
    • 80455174620 scopus 로고    scopus 로고
    • Orientation-specific signalling by thrombopoietin receptor dimers
    • doi: 10.1038/emboj.2011.315; pmid: 21892137
    • J. Staerk et al., Orientation-specific signalling by thrombopoietin receptor dimers. EMBO J. 30, 4398-4413 (2011). doi: 10.1038/emboj.2011.315; pmid: 21892137
    • (2011) EMBO J. , vol.30 , pp. 4398-4413
    • Staerk, J.1
  • 51
    • 0027473576 scopus 로고
    • Signal transduction mediated by growth hormone receptor and its chimeric molecules with the granulocyte colony-stimulating factor receptor
    • doi: 10.1073/pnas.90.1.123; pmid: 7678333
    • E. Ishizaka-Ikeda, R. Fukunaga, W. I. Wood, D. V. Goeddel, S. Nagata, 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 (1993). doi: 10.1073/pnas.90.1.123; pmid: 7678333
    • (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
  • 52
    • 0037033012 scopus 로고    scopus 로고
    • The pseudokinase domain is required for suppression of basal activity of Jak2 and Jak3 tyrosine kinases and for cytokine-inducible activation of signal transduction
    • doi: 10.1074/jbc.M205156200; pmid: 12351625
    • P. Saharinen, O. Silvennoinen, The pseudokinase domain is required for suppression of basal activity of Jak2 and Jak3 tyrosine kinases and for cytokine-inducible activation of signal transduction. J. Biol. Chem. 277, 47954-47963 (2002). doi: 10.1074/jbc.M205156200; pmid: 12351625
    • (2002) J. Biol. Chem. , vol.277 , pp. 47954-47963
    • Saharinen, P.1    Silvennoinen, O.2
  • 53
    • 0036762867 scopus 로고    scopus 로고
    • Prediction of the structure of human Janus kinase 2 (JAK2) comprising JAK homology domains 1 through 7
    • doi: 10.1093/protein/15.9.727; pmid: 12456871
    • F. Giordanetto, R. T. Kroemer, Prediction of the structure of human Janus kinase 2 (JAK2) comprising JAK homology domains 1 through 7. Protein Eng. 15, 727-737 (2002). doi: 10.1093/protein/15.9.727; pmid: 12456871
    • (2002) Protein Eng. , vol.15 , pp. 727-737
    • Giordanetto, F.1    Kroemer, R.T.2
  • 54
    • 28444493656 scopus 로고    scopus 로고
    • Crosstalk in G protein-coupled receptors: Changes at the transmembrane homodimer interface determine activation
    • doi: 10.1073/pnas.0508950102; pmid: 16301531
    • W. Guo, L. Shi, M. Filizola, H. Weinstein, J. A. Javitch, Crosstalk in G protein-coupled receptors: Changes at the transmembrane homodimer interface determine activation. Proc. Natl. Acad. Sci. U.S.A. 102, 17495-17500 (2005). doi: 10.1073/pnas.0508950102; pmid: 16301531
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 17495-17500
    • Guo, W.1    Shi, L.2    Filizola, M.3    Weinstein, H.4    Javitch, J.A.5
  • 55
    • 34548561606 scopus 로고    scopus 로고
    • A FRET map of membrane anchors suggests distinct microdomains of heterotrimeric G proteins
    • doi: 10.1242/jcs.001404; pmid: 17690305
    • D. Abankwa, H. Vogel, A FRET map of membrane anchors suggests distinct microdomains of heterotrimeric G proteins. J. Cell Sci. 120, 2953-2962 (2007). doi: 10.1242/jcs.001404; pmid: 17690305
    • (2007) J. Cell Sci. , vol.120 , pp. 2953-2962
    • Abankwa, D.1    Vogel, H.2


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