Regulation of JAKs: Insights gleaned from the functional protein domains

Jak-Stat Signaling: From Basics to Disease

Volumn , Issue , 2012, Pages 5-25

  Haan, Claude ^a   Ungureanu, Daniela ^b,c   Pekkala, Tuija ^b,c   Silvennoinen, Olli ^b,c   Haan, Serge ^a  

^a UNIVERSITY OF LUXEMBOURG   (Luxembourg)

^b TAMPERE UNIVERSITY OF TECHNOLOGY   (Finland)

^c TAMPERE UNIVERSITY HOSPITAL   (Finland)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 84882772873     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1007/978-3-7091-0891-8_2     Document Type: Chapter

References (120)

1. Adelaide J, Perot C, Gelsi-Boyer V, Pautas C, Murati A, Copie-Bergman C, ImbertM, Chaffanet M, Birnbaum D, Mozziconacci MJ (2006) A t(8;9) translocation with PCM1-JAK2 fusion in a patient with T-cell lymphoma. Leukemia 20(3):536-537
2. Argetsinger LS, Kouadio JL, Steen H, Stensballe A, Jensen ON, Carter-Su C (2004) Autophosphorylation of JAK2 on tyrosines 221 and 570 regulates its activity. Mol Cell Biol 24(11):4955-4967
3. Autissier P, De Vos J, Liautard J, Tupitsyn N, Jacquet C, Chavdia N, Klein B, Brochier J, Gaillard JP (1998) Dimerization and activation of the common transducing chain (gp130) of the cytokines of the IL-6 family by mAb. Int Immunol 10(12):1881-1889
4. Baxter EJ, Scott LM, Campbell PJ, East C, Fourouclas N, Swanton S, Vassiliou GS, Bench AJ, Boyd EM, Curtin N, Scott MA, Erber WN, Green AR (2005) Acquired mutation of the tyrosine kinase JAK2 in human myeloproliferative disorders. Lancet 365(9464):1054-1061
5. Behrmann I, Smyczek T, Heinrich PC, Schmitz-Van de Leur H, Komyod W, Giese B, Muller-Newen G, Haan S, Haan C (2004) Janus kinase (Jak) subcellular localization revisited: The exclusive membrane localization of endogenous Janus kinase 1 by cytokine receptor interaction uncovers the Jak.receptor complex to be equivalent to a receptor tyrosine kinase. J Biol Chem 279(34):35486-35493
6. Bercovich D, Ganmore I, Scott LM, Wainreb G, Birger Y, Elimelech A, Shochat C, Cazzaniga G, Biondi A, Basso G, Cario G, Schrappe M, Stanulla M, Strehl S, Haas OA, Mann G, Binder V, Borkhardt A, Kempski H, Trka J, Bielorei B, Avigad S, Stark B, Smith O, Dastugue N, Bourquin JP, Tal NB, Green AR, Izraeli S (2008) Mutations of JAK2 in acute lymphoblastic leukaemias associated with Down's syndrome. Lancet 372(9648):1484-1492
7. Boggon TJ, Li Y, Manley PW, Eck MJ (2005) Crystal structure of the Jak3 kinase domain in complex with a staurosporine analog. Blood 106(3):996-1002
8. Boudeau J, Miranda-Saavedra D, Barton GJ, Alessi DR (2006) Emerging roles of pseudokinases. Trends Cell Biol 16(9):443-452
9. Bousquet M, Quelen C, De Mas V, Duchayne E, Roquefeuil B, Delsol G, Laurent G, Dastugue N, Brousset P (2005) The t(8;9)(p22;p24) translocation in atypical chronic myeloid leukaemia yields a new PCM1-JAK2 fusion gene. Oncogene 24(48):7248-7252
10. Cacalano NA, Migone TS, Bazan F, Hanson EP, Chen M, Candotti F, O'Shea JJ, Johnston JA (1999) Autosomal SCID caused by a point mutation in the N-terminus of Jak3: mapping of the Jak3-receptor interaction domain. EMBO J 18(6):1549-1558
11. Candotti F, Oakes SA, Johnston JA, Giliani S, Schumacher RF, Mella P, Fiorini M, Ugazio AG, Badolato R, Notarangelo LD, Bozzi F, Macchi P, Strina D, Vezzoni P, Blaese RM, O'Shea JJ, Villa A (1997) Structural and functional basis for JAK3-deficient severe combined immunodeficiency. Blood 90(10):3996-4003
12. Chen M, Cheng A, Chen YQ, Hymel A, Hanson EP, Kimmel L, Minami Y, Taniguchi T, Changelian PS, O'Shea JJ (1997) The amino terminus of JAK3 is necessary and sufficient for binding to the common gamma chain and confers the ability to transmit interleukin 2-mediated signals. Proc Natl Acad Sci USA 94(13):6910-6915
13. Chen M, Cheng A, Candotti F, Zhou YJ, Hymel A, Fasth A, Notarangelo LD, O'Shea JJ (2000) Complex effects of naturally occurring mutations in the JAK3 pseudokinase domain: evidence for interactions between the kinase and pseudokinase domains. Mol Cell Biol 20(3):947-956
14. Cirmena G, Aliano S, Fugazza G, Bruzzone R, Garuti A, Bocciardi R, Bacigalupo A, Ravazzolo R, Ballestrero A, Sessarego M (2008) A BCR-JAK2 fusion gene as the result of a t(9;22)(p24; q11) in a patient with acute myeloid leukemia. Cancer Genet Cytogenet 183(2):105-108
15. Constantinescu SN, Huang LJ, Nam H, Lodish HF (2001) The erythropoietin receptor cytosolic juxtamembrane domain contains an essential, precisely oriented, hydrophobic motif. Mol Cell 7(2):377-385
16. Dusa A, Staerk J, Elliott J, Pecquet C, Poirel HA, Johnston JA, Constantinescu SN (2008) Substitution of pseudokinase domain residue Val-617 by large non-polar amino acids causes activation of JAK2. J Biol Chem 283(19):12941-12948
17. Dusa A, Mouton C, Pecquet C, Herman M, Constantinescu SN (2010) JAK2 V617F constitutive activation requires JH2 residue F595: A pseudokinase domain target for specific inhibitors. PLoS One 5(6):e11157
18. Eswaran J, Patnaik D, Filippakopoulos P, Wang F, Stein RL, Murray JW, Higgins JM, Knapp S (2009) Structure and functional characterization of the atypical human kinase haspin. Proc Natl Acad Sci USA 106(48):20198-20203
19. Feener EP, Rosario F, Dunn SL, Stancheva Z, Myers MG Jr (2004) Tyrosine phosphorylation of Jak2 in the JH2 domain inhibits cytokine signaling. Mol Cell Biol 24(11):4968-4978
20. Flex E, Petrangeli V, Stella L, Chiaretti S, Hornakova T, Knoops L, Ariola C, Fodale V, Clappier E, Paoloni F,Martinelli S, Fragale A, SanchezM, Tavolaro S,Messina M, Cazzaniga G, Camera A, Pizzolo G, Tornesello A, Vignetti M, Battistini A, Cave H, Gelb BD, Renauld JC, Biondi A, Constantinescu SN, Foa R, Tartaglia M (2008) Somatically acquired JAK1 mutations in adult acute lymphoblastic leukemia. J Exp Med 205(4):751-758
21. Funakoshi-Tago M, Pelletier S, Matsuda T, Parganas E, Ihle JN (2006) Receptor specific downregulation of cytokine signaling by autophosphorylation in the FERM domain of Jak2. EMBO J 25(20):4763-4772
22. Gauzzi MC, Barbieri G, Richter MF, Uze G, Ling L, Fellous M, Pellegrini S (1997) The aminoterminal region of Tyk2 sustains the level of interferon alpha receptor 1, a component of the interferon alpha/beta receptor. Proc Natl Acad Sci USA 94(22):11839-11844
23. Ghoreschi K, Laurence A, O'Shea JJ (2009) Janus kinases in immune cell signaling. Immunol Rev 228(1):273-287
24. Giese B, Au-Yeung CK, Herrmann A, Diefenbach S, Haan C, Kuster A,Wortmann SB, Roderburg C, Heinrich PC, Behrmann I, Muller-Newen G (2003) Long term association of the cytokine receptor gp130 and the Janus kinase Jak1 revealed by FRAP analysis. J Biol Chem 278(40): 39205-39213
25. Girault JA, Labesse G, Mornon JP, Callebaut I (1998) Janus kinases and focal adhesion kinases play in the 4.1 band: A superfamily of band 4.1 domains important for cell structure and signal transduction. Mol Med 4(12):751-769
26. Gorantla SP, Dechow TN, Grundler R, Illert AL, Zum Buschenfelde CM, Kremer M, Peschel C, Duyster J (2010) Oncogenic JAK2V617F requires an intact SH2-like domain for constitutive activation and induction of a myeloproliferative disease in mice. Blood 116(22):4600-4611. doi:blood-2009-07-236133
27. Greiser JS, Stross C, Heinrich PC, Behrmann I, Hermanns HM (2002) Orientational constraints of the gp130 intracellular juxtamembrane domain for signaling. J Biol Chem 277 (30):26959-26965
28. Griesinger F, Hennig H, Hillmer F, Podleschny M, Steffens R, Pies A, Wormann B, Haase D, Bohlander SK (2005) A BCR-JAK2 fusion gene as the result of a t(9;22)(p24;q11.2) translocation in a patient with a clinically typical chronic myeloid leukemia. Genes Chromosomes Cancer 44(3):329-333. doi:10.1002/gcc.20235
29. Haan C, Is'harc H, Hermanns HM, Schmitz-Van De Leur H, Kerr IM, Heinrich PC, Grotzinger J, Behrmann I (2001) Mapping of a region within the N terminus of Jak1 involved in cytokine receptor interaction. J Biol Chem 276(40):37451-37458
30. Haan C, Heinrich PC, Behrmann I (2002) Structural requirements of the interleukin-6 signal transducer gp130 for its interaction with Janus kinase 1: The receptor is crucial for kinase activation. Biochem J 361(Pt 1):105-111
31. Haan C, Kreis S, Margue C, Behrmann I (2006) Jaks and cytokine receptors-An intimate relationship. Biochem Pharmacol 72(11):1538-1546
32. Haan S, Margue C, Engrand A, Rolvering C, Schmitz-Van de Leur H, Heinrich PC, Behrmann I, Haan C (2008) Dual role of the Jak1 FERM and kinase domains in cytokine receptor binding and in stimulation-dependent Jak activation. J Immunol 180(2):998-1007
33. Haan C, Kroy DC,Wuller S, Sommer U, Nocker T, Rolvering C, Behrmann I, Heinrich PC, Haan S (2009) An unusual insertion in Jak2 is crucial for kinase activity and differentially affects cytokine responses. J Immunol 182(5):2969-2977
34. Haan C, Behrmann I, Haan S (2010) Perspectives for the use of structural information and chemical genetics to develop inhibitors of Janus kinases. J Cell Mol Med 14(3):504-527
35. Hamada K, Shimizu T,Matsui T, Tsukita S, Hakoshima T (2000) Structural basis of the membranetargeting and unmasking mechanisms of the radixin FERMdomain. EMBO J 19(17):4449-4462
36. He K, Loesch K, Cowan JW, Li X, Deng L, Wang X, Jiang J, Frank SJ (2005) Janus kinase 2 enhances the stability of the mature growth hormone receptor. Endocrinology 146 (11):4755-4765
37. Heinrich PC, Behrmann I, Haan S, Hermanns HM, Muller-Newen G, Schaper F (2003) Principles of interleukin (IL)-6-type cytokine signalling and its regulation. Biochem J 374(Pt 1):1-20
38. Hilkens CM, Is'harc H, Lillemeier BF, Strobl B, Bates PA, Behrmann I, Kerr IM (2001) A region encompassing the FERM domain of Jak1 is necessary for binding to the cytokine receptor gp130. FEBS Lett 505(1):87-91
39. Hintzen C, Haan C, Tuckermann JP, Heinrich PC, Hermanns HM (2008) Oncostatin M-induced and constitutive activation of the JAK2/STAT5/CIS pathway suppresses CCL1, but not CCL7 and CCL8, chemokine expression. J Immunol 181(10):7341-7349
40. Huang LJ, Constantinescu SN, Lodish HF (2001) The N-terminal domain of Janus kinase 2 is required for Golgi processing and cell surface expression of erythropoietin receptor. Mol Cell 8 (6):1327-1338
41. Hubbard SR, Mohammadi M, Schlessinger J (1998) Autoregulatory mechanisms in proteintyrosine kinases. J Biol Chem 273(20):11987-11990
42. Ihle JN, Kerr IM (1995) Jaks and Stats in signaling by the cytokine receptor superfamily. Trends Genet 11(2):69-74
43. Ishida-Takahashi R, Rosario F, Gong Y, Kopp K, Stancheva Z, Chen X, Feener EP, Myers MG Jr (2006) Phosphorylation of Jak2 on Ser(523) inhibits Jak2-dependent leptin receptor signaling. Mol Cell Biol 26(11):4063-4073. doi:26/11/4063
44. James C, Ugo V, Le Couedic JP, Staerk J, Delhommeau F, Lacout C, Garcon L, Raslova H, Berger R, Bennaceur-Griscelli A, Villeval JL, Constantinescu SN, Casadevall N, Vainchenker W (2005) A unique clonal JAK2 mutation leading to constitutive signalling causes polycythaemia vera. Nature 434(7037):1144-1148
45. Jeong EG, Kim MS, Nam HK, Min CK, Lee S, Chung YJ, Yoo NJ, Lee SH (2008) Somatic mutations of JAK1 and JAK3 in acute leukemias and solid cancers. Clin Cancer Res 14 (12):3716-3721
46. Jura N, Shan Y, Cao X, Shaw DE, Kuriyan J (2009) Structural analysis of the catalytically inactive kinase domain of the human EGF receptor 3. Proc Natl Acad Sci USA 106(51):21608-21613. doi:0912101106
47. Kamizono S, Hanada T, Yasukawa H, Minoguchi S, Kato R, Minoguchi M, Hattori K, Hatakeyama S, Yada M, Morita S, Kitamura T, Kato H, Nakayama K, Yoshimura A (2001) The SOCS box of SOCS-1 accelerates ubiquitin-dependent proteolysis of TEL-JAK2. J Biol Chem 276(16):12530-12538
48. Karaghiosoff M, Neubauer H, Lassnig C, Kovarik P, Schindler H, Pircher H, McCoy B, Bogdan C, Decker T, Brem G, Pfeffer K, Muller M (2000) Partial impairment of cytokine responses in Tyk2-deficient mice. Immunity 13(4):549-560
49. Kohlhuber F, Rogers NC, Watling D, Feng J, Gushin D, Briscoe J, Witthuhn BA, Kotenko SV, Pestka S, Stark GR, Ihle JN, Kerr IM (1997) A JAK1/JAK2 chimera can sustain alpha and gamma interferon responses. Mol Cell Biol 17:695-706
50. Kovanen PE, Leonard WJ (2004) Cytokines and immunodeficiency diseases: critical roles of the gamma(c)-dependent cytokines interleukins 2, 4, 7, 9, 15, and 21, and their signaling pathways. Immunol Rev 202:67-83
51. Kralovics R, Passamonti F, Buser AS, Teo SS, Tiedt R, Passweg JR, Tichelli A, Cazzola M, Skoda RC (2005) A gain-of-function mutation of JAK2 in myeloproliferative disorders. N Engl J Med 352(17):1779-1790
52. Kratz CP, Boll S, Kontny U, Schrappe M, Niemeyer CM, Stanulla M (2006) Mutational screen reveals a novel JAK2 mutation, L611S, in a child with acute lymphoblastic leukemia. Leukemia 20(2):381-383
53. Kubatzky KF, Liu W, Goldgraben K, Simmerling C, Smith SO, Constantinescu SN (2005) Structural requirements of the extracellular to transmembrane domain junction for erythropoietin receptor function. J Biol Chem 280(15):14844-14854
54. Kurzer JH, Argetsinger LS, Zhou YJ, Kouadio JL, O'Shea JJ, Carter-Su C (2004) Tyrosine 813 is a site of JAK2 autophosphorylation critical for activation of JAK2 by SH2-B beta. Mol Cell Biol 24(10):4557-4570
55. Lacronique V, Boureux A, Valle VD, Poirel H, Quang CT, Mauchauffe M, Berthou C, Lessard M, Berger R, Ghysdael J, Bernard OA (1997) A TEL-JAK2 fusion protein with constitutive kinase activity in human leukemia. Science 278(5341):1309-1312
56. Lee TS, Ma W, Zhang X, Giles F, Kantarjian H, Albitar M (2009) Mechanisms of constitutive activation of Janus kinase 2-V617F revealed at the atomic level through molecular dynamics simulations. Cancer 115(8):1692-1700
57. Levine RL, Wadleigh M, Cools J, Ebert BL, Wernig G, Huntly BJ, Boggon TJ, Wlodarska I, Clark JJ, Moore S, Adelsperger J, Koo S, Lee JC, Gabriel S, Mercher T, D'Andrea A, Frohling S, Dohner K, Marynen P, Vandenberghe P, Mesa RA, Tefferi A, Griffin JD, Eck MJ, Sellers WR, Meyerson M, Golub TR, Lee SJ, Gilliland DG (2005) Activating mutation in the tyrosine kinase JAK2 in polycythemia vera, essential thrombocythemia, and myeloid metaplasia with myelofibrosis. Cancer Cell 7(4):387-397
58. Lindauer K, Loerting T, Liedl KR, Kroemer RT (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(1):27-37
59. Livnah O, Stura EA, Middleton SA, Johnson DL, Jolliffe LK, Wilson IA (1999) Crystallographic evidence for preformed dimers of erythropoietin receptor before ligand activation. Science 283:987-990
60. Lu X, Huang LJ, Lodish HF (2008) Dimerization by a cytokine receptor is necessary for constitutive activation of JAK2V617F. J Biol Chem 283(9):5258-5266
61. Lucet IS, Fantino E, Styles M, Bamert R, Patel O, Broughton SE, Walter M, Burns CJ, Treutlein H, Wilks AF, Rossjohn J (2006) The structural basis of Janus kinase 2 inhibition by a potent and specific pan-Janus kinase inhibitor. Blood 107(1):176-183
62. Luo H, Rose P, Barber D, Hanratty WP, Lee S, Roberts TM, D'Andrea AD, Dearolf CR (1997) Mutation in the Jak kinase JH2 domain hyperactivates Drosophila and mammalian Jak-Stat pathways. Mol Cell Biol 17(3):1562-1571
63. Macchi P, Villa A, Giliani S, Sacco MG, Frattini A, Porta F, Ugazio AG, Johnston JA, Candotti F, O'Shea JJ et al (1995) Mutations of Jak-3 gene in patients with autosomal severe combined immune deficiency (SCID). Nature 377(6544):65-68
64. Malinge S, Ragu C, Della-Valle V, Pisani D, Constantinescu SN, Perez C, Villeval JL, Reinhardt D, Landman-Parker J, Michaux L, Dastugue N, Baruchel A, Vainchenker W, Bourquin JP, Penard-Lacronique V, Bernard OA (2008) Activating mutations in human acute megakaryoblastic leukemia. Blood 112(10):4220-4226
65. Manning BD, Cantley LC (2002) Hitting the target: emerging technologies in the search for kinase substrates. Sci STKE 2002(162):PE49
66. Mazurkiewicz-Munoz AM, Argetsinger LS, Kouadio JL, Stensballe A, Jensen ON, Cline JM, Carter-Su C (2006) Phosphorylation of JAK2 at serine 523: A negative regulator of JAK2 that is stimulated by growth hormone and epidermal growth factor. Mol Cell Biol 26(11):4052-4062
67. Mercher T, Wernig G, Moore SA, Levine RL, Gu TL, Frohling S, Cullen D, Polakiewicz RD, Bernard OA, Boggon TJ, Lee BH, Gilliland DG (2006) JAK2T875N is a novel activating mutation that results in myeloproliferative disease with features of megakaryoblastic leukemia in a murine bone marrow transplantation model. Blood 108(8):2770-2779
68. Mukherjee K, Sharma M, Urlaub H, Bourenkov GP, Jahn R, Sudhof TC, Wahl MC (2008) CASK functions as a Mg2+-independent neurexin kinase. Cell 133(2):328-339
69. Muller-Newen G, Kuster A, Wijdenes J, Schaper F, Heinrich PC (2000) Studies on the interleukin-6-type cytokine signal transducer gp130 reveal a novel mechanism of receptor activation by monoclonal antibodies. J Biol Chem 275(7):4579-4586
70. Murati A, Gelsi-Boyer V, Adelaide J, Perot C, Talmant P, Giraudier S, Lode L, Letessier A, Delaval B, Brunel V, ImbertM, Garand R, Xerri L, Birnbaum D, Mozziconacci MJ, ChaffanetM (2005) PCM1-JAK2 fusion in myeloproliferative disorders and acute erythroid leukemia with t(8;9) translocation. Leukemia 19(9):1692-1696
71. Neubauer H, Cumano A, Muller M, Wu H, Huffstadt U, Pfeffer K (1998) Jak2 deficiency defines an essential developmental checkpoint in definitive hematopoiesis. Cell 93(3):397-409
72. Nishii K, Nanbu R, Lorenzo VF, Monma F, Kato K, Ryuu H, Katayama N (2007) Expression of the JAK2 V617F mutation is not found in de novo AML and MDS but is detected in MDSderived leukemia of megakaryoblastic nature. Leukemia 21(6):1337-1338
73. Nosaka T, van Deursen JM, Tripp RA, Thierfelder WE, Witthuhn BA, McMickle AP, Doherty PC, Grosveld GC, Ihle JN (1995) Defective lymphoid development in mice lacking Jak3. Science 270(5237):800-802
74. O'Sullivan LA, Liongue C, Lewis RS, Stephenson SE, Ward AC (2007) Cytokine receptor signaling through the Jak-Stat-Socs pathway in disease. Mol Immunol 44(10):2497-2506
75. Parganas E, Wang D, Stravopodis D, Topham DJ, Marine JC, Teglund S, Vanin EF, Bodner S, Colamonici OR, van Deursen JM, Grosveld G, Ihle JN (1998) Jak2 is essential for signaling through a variety of cytokine receptors. Cell 93(3):385-395
76. Park SY, Saijo K, Takahashi T, Osawa M, Arase H, Hirayama N, Miyake K, Nakauchi H, Shirasawa T, Saito T (1995) Developmental defects of lymphoid cells in Jak3 kinase-deficient mice. Immunity 3(6):771-782
77. Pearson MA, Reczek D, Bretscher A, Karplus PA (2000) Structure of the ERM protein moesin reveals the FERM domain fold masked by an extended actin binding tail domain. Cell 101 (3):259-270
78. Peeters P, Raynaud SD, Cools J, Wlodarska I, Grosgeorge J, Philip P,Monpoux F, Van Rompaey L, BaensM, Van den Berghe H,Marynen P (1997) Fusion of TEL, the ETS-variant gene 6 (ETV6), to the receptor-associated kinase JAK2 as a result of t(9;12) in a lymphoid and t(9;15;12) in a myeloid leukemia. Blood 90(7):2535-2540
79. Pestka S, Krause CD, Walter MR (2004) Interferons, interferon-like cytokines, and their receptors. Immunol Rev 202:8-32
80. Pesu M, Candotti F, Husa M, Hofmann SR, Notarangelo LD, O'Shea JJ (2005) Jak3, severe combined immunodeficiency, and a new class of immunosuppressive drugs. Immunol Rev 203:127-142
81. Pesu M, Laurence A, Kishore N, Zwillich SH, Chan G, O'Shea JJ (2008) Therapeutic targeting of Janus kinases. Immunol Rev 223:132-142
82. Poitras JL, Dal Cin P, Aster JC, Deangelo DJ, Morton CC (2008) Novel SSBP2-JAK2 fusion gene resulting from a t(5;9)(q14.1;p24.1) in pre-B acute lymphocytic leukemia. Genes Chromosomes Cancer 47(10):884-889
83. Radtke S, Hermanns HM, Haan C, Schmitz-Van De Leur H, Gascan H, Heinrich PC, Behrmann I (2002) Novel role of Janus kinase 1 in the regulation of oncostatin M receptor surface expression. J Biol Chem 277(13):11297-11305
84. Radtke S, Haan S, Jorissen A, Hermanns HM, Diefenbach S, Smyczek T, Schmitz-Vandeleur H, Heinrich PC, Behrmann I, Haan C (2005) The Jak1 SH2 domain does not fulfill a classical SH2 function in Jak/STAT signaling but plays a structural role for receptor interaction and upregulation of receptor surface expression. J Biol Chem 280(27):25760-25768
85. Radtke S, Jorissen A, Schmitz-Van de Leur H, Heinrich PC, Behrmann I (2006) Three dileucinelike motifs within the interbox1/2 region of the human oncostatin M receptor prevent efficient surface expression in absence of an associated Janus kinase. J Biol Chem 281(7):4024-4034
86. Ragimbeau J, Dondi E, Alcover A, Eid P, Uze G, Pellegrini S (2003) The tyrosine kinase Tyk2 controls IFNAR1 cell surface expression. EMBO J 22(3):537-547
87. Reiter A, Walz C, Watmore A, Schoch C, Blau I, Schlegelberger B, Berger U, Telford N, Aruliah S, Yin JA, Vanstraelen D, Barker HF, Taylor PC, O'Driscoll A, Benedetti F, Rudolph C, Kolb HJ, Hochhaus A, Hehlmann R, Chase A, Cross NC (2005) The t(8;9)(p22;p24) is a recurrent abnormality in chronic and acute leukemia that fuses PCM1 to JAK2. Cancer Res 65(7): 2662-2667
88. Remy I, Wilson IA, Michnick SW (1999) Erythropoietin receptor activation by a ligand-induced conformation change. Science 283(5404):990-993
89. Richter MF, Dumenil G, Uze G, Fellous M, Pellegrini S (1998) Specific contribution of Tyk2 JH regions to the binding and the expression of the interferon alpha/beta receptor component IFNAR1. J Biol Chem 273(38):24723-24729
90. Rishton GM (2003) Nonleadlikeness and leadlikeness in biochemical screening. Drug Discov Today 8(2):86-96
91. Robertson SA, Koleva RI, Argetsinger LS, Carter-Su C, Marto JA, Feener EP, Myers MG Jr (2009) Regulation of Jak2 function by phosphorylation of Tyr317 and Tyr637 during cytokine signaling. Mol Cell Biol 29(12):3367-3378
92. Rodig SJ, Meraz MA, White JM, Lampe PA, Riley JK, Arthur CD, King KL, Sheehan KC, Yin L, Pennica D, Johnson EM Jr, Schreiber RD (1998) Disruption of the Jak1 gene demonstrates obligatory and nonredundant roles of the Jaks in cytokine-induced biologic responses. Cell 93 (3):373-383
93. Royer Y, Staerk J, Costuleanu M, Courtoy PJ, Constantinescu SN (2005) Janus kinases affect thrombopoietin receptor cell surface localization and stability. J Biol Chem 280 (29):27251-27261
94. Russell SM, Tayebi N, Nakajima H, Riedy MC, Roberts JL, Aman MJ, Migone TS, Noguchi M, Markert ML, Buckley RH et al (1995) Mutation of Jak3 in a patient with SCID: essential role of Jak3 in lymphoid development. Science 270(5237):797-800
95. Saharinen P, Silvennoinen O (2002) 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(49):47954-47963
96. Saharinen P, Takaluoma K, Silvennoinen O (2000) Regulation of the Jak2 tyrosine kinase by its pseudokinase domain. Mol Cell Biol 20(10):3387-3395
97. Saharinen P, Vihinen M, Silvennoinen O (2003) Autoinhibition of Jak2 tyrosine kinase is dependent on specific regions in its pseudokinase domain. Mol Biol Cell 14(4):1448-1459
98. Scheeff ED, Eswaran J, Bunkoczi G, Knapp S, Manning G (2009) Structure of the pseudokinase VRK3 reveals a degraded catalytic site, a highly conserved kinase fold, and a putative regulatory binding site. Structure 17(1):128-138
99. Shaw MH, Boyartchuk V, Wong S, Karaghiosoff M, Ragimbeau J, Pellegrini S, Muller M, Dietrich WF, Yap GS (2003) A natural mutation in the Tyk2 pseudokinase domain underlies altered susceptibility of B10.Q/J mice to infection and autoimmunity. Proc Natl Acad Sci USA 100(20):11594-11599
100. Shi F, Telesco SE, Liu Y, Radhakrishnan R, Lemmon MA (2010) ErbB3/HER3 intracellular domain is competent to bind ATP and catalyze autophosphorylation. Proc Natl Acad Sci USA 107(17):7692-7697
101. Shimoda K, Kato K, Aoki K, Matsuda T, Miyamoto A, Shibamori M, Yamashita M, Numata A, Takase K, Kobayashi S, Shibata S, Asano Y, Gondo H, Sekiguchi K, Nakayama K, Nakayama T, Okamura T, Okamura S, Niho Y (2000) Tyk2 plays a restricted role in IFN alpha signaling, although it is required for IL-12-mediated T cell function. Immunity 13(4):561-571
102. Siewert E, Muller-Esterl W, Starr R, Heinrich PC, Schaper F (1999) Different protein turnover of interleukin-6-type cytokine signalling components. Eur J Biochem 265:251-257
103. Sigurdsson S, Nordmark G, Goring HH, Lindroos K, Wiman AC, Sturfelt G, Jonsen A, Rantapaa-Dahlqvist S, Moller B, Kere J, Koskenmies S, Widén E, Eloranta ML, Julkunen H, Kristjansdottir H, Steinsson K, Alm G, Ronnblom L, Syvanen AC (2005) Polymorphisms in the tyrosine kinase 2 and interferon regulatory factor 5 genes are associated with systemic lupus erythematosus. Am J Hum Genet 76(3):528-537
104. Thomis DC, Gurniak CB, Tivol E, Sharpe AH, Berg LJ (1995) Defects in B lymphocyte maturation and T lymphocyte activation in mice lacking Jak3. Science 270(5237):794-797
105. Ungureanu D, Saharinen P, Junttila I, Hilton DJ, Silvennoinen O (2002) Regulation of Jak2 through the ubiquitin-proteasome pathway involves phosphorylation of Jak2 on Y1007 and interaction with SOCS-1. Mol Cell Biol 22(10):3316-3326
106. Walters DK, Mercher T, Gu TL, O'Hare T, Tyner JW, Loriaux M, Goss VL, Lee KA, Eide CA, Wong MJ, Stoffregen EP, McGreevey L, Nardone J, Moore SA, Crispino J, Boggon TJ, Heinrich MC, Deininger MW, Polakiewicz RD, Gilliland DG, Druker BJ (2006) Activating alleles of JAK3 in acute megakaryoblastic leukemia. Cancer Cell 10(1):65-75
107. Watowich SS, Liu KD, Xie X, Lai SY, Mikami A, Longmore GD, Goldsmith MA (1999) Oligomerization and scaffolding functions of the erythropoietin receptor cytoplasmic tail. J Biol Chem 274(9):5415-5421
108. Wernig G, Gonneville JR, Crowley BJ, Rodrigues MS, Reddy MM, Hudon HE, Walz C, Reiter A, Podar K, Royer Y, Constantinescu SN, Tomasson MH, Griffin JD, Gilliland DG, Sattler M (2008) The Jak2V617F oncogene associated with myeloproliferative diseases requires a functional FERM domain for transformation and for expression of the Myc and Pim protooncogenes. Blood 111(7):3751-3759
109. Wilks AF, Harpur AG, Kurban RR, Ralph SJ, Zurcher G, Ziemiecki A (1991) Two novel proteintyrosine kinases, each with a second phosphotransferase-related catalytic domain, define a new class of protein kinase. Mol Cell Biol 11(4):2057-2065
110. Williams NK, Bamert RS, Patel O, Wang C, Walden PM, Wilks AF, Fantino E, Rossjohn J, Lucet IS (2009) Dissecting specificity in the Janus kinases: The structures of JAK-specific inhibitors complexed to the JAK1 and JAK2 protein tyrosine kinase domains. J Mol Biol 387(1):219-232
111. Yasukawa H, Misawa H, Sakamoto H, Masuhara M, Sasaki A, Wakioka T, Ohtsuka S, Imaizumi T, Matsuda T, Ihle JN, Yoshimura A (1999) The JAK-binding protein JAB inhibits Janus tyrosine kinase activity through binding in the activation loop. EMBO J 18(5):1309-1320
112. Yeh TC, Pellegrini S (1999) The Janus kinase family of protein tyrosine kinases and their role in signaling. Cell Mol Life Sci 55(12):1523-1534
113. Yeh TC, Dondi E, Uze G, Pellegrini S (2000) A dual role for the kinase-like domain of the tyrosine kinase Tyk2 in interferon-alpha signaling. Proc Natl Acad Sci USA 97(16):8991-8996
114. Yoshimura A, Naka T, Kubo M (2007) SOCS proteins, cytokine signalling and immune regulation. Nat Rev Immunol 7(6):454-465
115. Zeqiraj E, van Aalten DM (2010) Pseudokinases-remnants of evolution or key allosteric regulators? Curr Opin Struct Biol 20(6):772-781
116. Zeqiraj E, Filippi BM, Deak M, Alessi DR, van Aalten DM (2009) Structure of the LKB1-STRAD-MO25 complex reveals an allosteric mechanism of kinase activation. Science 326 (5960):1707-1711
117. Zhao Y, Wagner F, Frank SJ, Kraft AS (1995) The amino-terminal portion of the JAK2 protein kinase is necessary for binding and phosphorylation of the granulocyte-macrophage colonystimulating factor receptor beta c chain. J Biol Chem 270(23):13814-13818
118. Zhao R, Xing S, Li Z, Fu X, Li Q, Krantz SB, Zhao ZJ (2005) Identification of an acquired JAK2 mutation in polycythemia vera. J Biol Chem 280(24):22788-22792
119. Zhou YJ, Chen M, Cusack NA, Kimmel LH, Magnuson KS, Boyd JG, Lin W, Roberts JL, Lengi A, Buckley RH, Geahlen RL, Candotti F, Gadina M, Changelian PS, O'Shea JJ (2001) Unexpected effects of FERM domain mutations on catalytic activity of Jak3: structural implication for Janus kinases. Mol Cell 8(5):959-969
120. Zhu HJ, Sizeland AM (1999) A pivotal role for the transmembrane domain in transforming growth factor-beta receptor activation. J Biol Chem 274(17):11773-11781