Cross-regulation of JAK and Src kinases

References

• Argetsinger L, Campbell G, Yang X, Witthuhn B, Silvennoinen O, Ihle J, Carter-Su C. Identification of JAK2 as a growth hormone receptor-associated tyrosine kinase. Cell 1993; 74: 237–244
   PubMed Web of Science ®Google Scholar
• Baxter EJ, Scott LM, Campbell PJ, East C, Fourouclas N, Swanton S, Vassiliou GS, Bench AJ, Boyd EM, Curtin N, et al. Acquired mutation of the tyrosine kinase JAK2 in human myeloproliferative disorders. Lancet 2005; 365: 1054–1061
   PubMed Web of Science ®Google Scholar
• Bowman T, Broome MA, Sinibaldi D, Wharton W, Pledger WJ, Sedivy JM, Irby R, Yeatman T, Courtneidge SA, Jove R. Stat3-mediated Myc expression is required for Src transformation and PDGF-induced mitogenesis. Proc Natl Acad Sci USA 2001; 98: 7319–7324
   PubMed Web of Science ®Google Scholar
• Brdicka T, Pavlistova D, Leo A, Bruyns E, Korinek V, Angelisova P, Scherer J, Shevchenko A, Hilgert I, Cerny J, et al. Phosphoprotein associated with glycosphingolipid-enriched microdomains (PAG), a novel ubiquitously expressed transmembrane adaptor protein, binds the protein tyrosine kinase csk and is involved in regulation of T cell activation. J Exp Med 2000; 191: 1591–1604
   PubMed Web of Science ®Google Scholar
• Cao X, Tay A, Guy GR, Tan YH. Activation and association of Stat3 with Src in v-Src-transformed cell lines. Mol Cell Biol 1996; 16: 1595–1603
   PubMed Web of Science ®Google Scholar
• Catlett-Falcone R, Dalton WS, Jove R. STAT proteins as novel targets for cancer therapy. Signal transducer an activator of transcription. Curr Opin Oncol 1999a; 11: 490–496
   PubMedGoogle Scholar
• Catlett-Falcone R, Landowski TH, Oshiro MM, Turkson J, Levitzki A, Savino R, Ciliberto G, Moscinski L, Fernandez-Luna JL, Nunez G, et al. Constitutive activation of Stat3 signaling confers resistance to apoptosis in human U266 myeloma cells. Immunity 1999b; 10: 105–115
   PubMed Web of Science ®Google Scholar
• Chaturvedi P, Reddy MV, Reddy EP. Src kinases and not JAKs activate STATs during IL-3 induced myeloid cell proliferation. Oncogene 1998; 16: 1749–1758
   PubMed Web of Science ®Google Scholar
• Chaturvedi P, Sharma S, Reddy EP. Abrogation of interleukin-3 dependence of myeloid cells by the v-src oncogene requires SH2 and SH3 domains which specify activation of STATs. Mol Cell Biol 1997; 17: 3295–3304
   PubMed Web of Science ®Google Scholar
• Chin H, Arai A, Wakao H, Kamiyama R, Miyasaka N, Miura O. Lyn physically associates with the erythropoietin receptor and may play a role in activation of the Stat5 pathway. Blood 1998; 91: 3734–3745
   PubMed Web of Science ®Google Scholar
• David M, Chen HE, Goelz S, Larner AC, Neel BG. Differential regulation of the alpha/beta interferon-stimulated Jak/Stat pathway by the SH2 domain-containing tyrosine phosphatase SHPTP1. Mol Cell Biol 1995; 15: 7050–7058
   PubMed Web of Science ®Google Scholar
• de la Chapelle A, Traskelin AL, Juvonen E. Truncated erythropoietin receptor causes dominantly inherited benign human erythrocytosis. Proc Natl Acad Sci USA 1993; 90: 4495–4499
   PubMed Web of Science ®Google Scholar
• De Sepulveda P, Okkenhaug K, Rose JL, Hawley RG, Dubreuil P, Rottapel R. Socs1 binds to multiple signalling proteins and suppresses steel factor-dependent proliferation. EMBO J 1999; 18: 904–915
   PubMed Web of Science ®Google Scholar
• Endo TA, Masuhara M, Yokouchi M, Suzuki R, Sakamoto H, Mitsui K, Matsumoto A, Tanimura S, Ohtsubo M, Misawa H, et al. A new protein containing an SH2 domain that inhibits JAK kinases. Nature 1997; 387: 921–924
   PubMed Web of Science ®Google Scholar
• Garcia R, Bowman TL, Niu G, Yu H, Minton S, Muro-Cacho CA, Cox CE, Falcone R, Fairclough R, Parsons S, et al. Constitutive activation of Stat3 by the Src and JAK tyrosine kinases participates in growth regulation of human breast carcinoma cells. Oncogene 2001; 20: 2499–2513
   PubMed Web of Science ®Google Scholar
• Harashima A, Suzuki M, Okochi A, Yamamoto M, Matsuo Y, Motoda R, Yoshioka T, Orita K. CD45 tyrosine phosphatase inhibits erythroid differentiation of umbilical cord blood CD34+ cells associated with selective inactivation of Lyn. Blood 2002; 100: 4440–4445
   PubMed Web of Science ®Google Scholar
• Harder KW, Quilici C, Naik E, Inglese M, Kountouri N, Turner A, Zlatic K, Tarlinton DM, Hibbs ML. Perturbed myelo/erythropoiesis in Lyn-deficient mice is similar to that in mice lacking the inhibitory phosphatases SHP-1 and SHIP-1. Blood 2004; 104: 3901–3910
   PubMed Web of Science ®Google Scholar
• Hermans MH, Antonissen C, Ward AC, Mayen AE, Ploemacher RE, Touw IP. Sustained receptor activation and hyperproliferation in response to granulocyte colony-stimulating factor (G-CSF) in mice with a severe congenital neutropenia/acute myeloid leukemia-derived mutation in the G-CSF receptor gene. J Exp Med 1999; 189: 683–692
   PubMed Web of Science ®Google Scholar
• Hibbs ML, Tarlinton DM, Armes J, Grail D, Hodgson G, Maglitto R, Stacker SA, Dunn AR. Multiple defects in the immune system of lyn-deficient mice, culminating in autoimmune disease. Cell 1995; 83: 301–311
   PubMed Web of Science ®Google Scholar
• Ho JM, Beattie BK, Squire JA, Frank DA, Barber DL. Fusion of the ets transcription factor TEL to Jak2 results in constitutive Jak-Stat signaling. Blood 1999; 93: 4354–4364
   PubMed Web of Science ®Google Scholar
• Hoefsloot LH, van Amelsvoort MP, Broeders LC, van der Plas DC, van Lom K, Hoogerbrugge H, Touw IP, Lowenberg B. Erythropoietin-induced activation of STAT5 is impaired in the myelodysplastic syndrome. Blood 1997; 89: 1690–1700
   PubMed Web of Science ®Google Scholar
• Hofmann S, Lam A, Frank S, Zhou Y, Ramos H, Kanno Y, Agnello D, Youle R, O'Shea J. Jak3-independent trafficking of the common gamma chain receptor subunit: Chaperone function of Jaks revisited. Mol Cell Biol 2004; 24: 5039–5049
   PubMed Web of Science ®Google Scholar
• Huang L, Constantinescu S, Lodish H. The N-terminal domain of Janus kinase 2 is required for Golgi processing and cell surface expression of erythropoietin receptor. Mol Cell 2001; 8: 1327–1338
   PubMed Web of Science ®Google Scholar
• Ingley E, Chappell D, Poon SY, Sarna MK, Beaumont JG, Williams JH, Stillitano JP, Tsai S, Leedman PJ, Tilbrook PA, Klinken SP. Thyroid hormone receptor-interacting protein 1 modulates cytokine and nuclear hormone signaling in erythroid cells. J Biol Chem 2001; 276: 43428–43434
   PubMed Web of Science ®Google Scholar
• Ingley E, McCarthy DJ, Pore JR, Sarna MK, Adenan AS, Wright MJ, Erber WN, Tilbrook PA, Klinken SP. Lyn deficiency reduces GATA-1, EKLF and STAT5, and induces extramedullary stress erythropoiesis. Oncogene 2005; 24: 336–343
   PubMed Web of Science ®Google Scholar
• Ingley E, Sarna MK, Beaumont JG, Tilbrook PA, Tsai S, Takemoto Y, Williams JH, Klinken SP. HS1 interacts with Lyn and is critical for erythropoietin-induced differentiation of erythroid cells. J Biol Chem 2000; 275: 7887–7893
   PubMed Web of Science ®Google Scholar
• James C, Ugo V, Le Couedic JP, Staerk J, Delhommeau F, Lacout C, Garcon L, Raslova H, Berger R, Bennaceur-Griscelli A, et al. A unique clonal JAK2 mutation leading to constitutive signalling causes polycythaemia vera. Nature 2005; 434: 1144–1148
   PubMed Web of Science ®Google Scholar
• Kamizono S, Hanada T, Yasukawa H, Minoguchi S, Kato R, Minoguchi M, Hattori K, Hatakeyama S, Yada M, Morita S, et al. The SOCS box of SOCS-1 accelerates ubiquitin-dependent proteolysis of TEL–JAK2. J Biol Chem 2001; 276: 12530–12538
   PubMed Web of Science ®Google Scholar
• Kawabuchi M, Satomi Y, Takao T, Shimonishi Y, Nada S, Nagai K, Tarakhovsky A, Okada M. Transmembrane phosphoprotein Cbp regulates the activities of Src-family tyrosine kinases. Nature 2000; 404: 999–1003
   PubMed Web of Science ®Google Scholar
• Kawaguchi Y, Kobayashi M, Tanabe A, Hara M, Nishi Y, Usui T, Nagai S, Nishibayashi Y, Nagao K, Yokoro K. Granulopoiesis in patients with congenital neutropenia. Am J Hematol 1985; 20: 223–234
   PubMed Web of Science ®Google Scholar
• Kawamura M, McVicar D, Johnston J, Blake T, Chen Y, Lal B, Lloyd A, Kelvin D, Staples J, Ortaldo J. Molecular cloning of L-JAK, a Janus family protein-tyrosine kinase expressed in natural killer cells and activated leukocytes. Proc Natl Acad Sci USA 1994; 91: 6374–6378
   PubMed Web of Science ®Google Scholar
• Kazansky AV, Rosen JM. Signal transducers and activators of transcription 5B potentiates v-Src-mediated transformation of NIH-3T3 cells. Cell Growth Differ 2001; 12: 1–7
   PubMedGoogle Scholar
• Klingmuller U, Lorenz U, Cantley LC, Neel BG, Lodish HF. Specific recruitment of SH-PTP1 to the erythropoietin receptor causes inactivation of JAK2 and termination of proliferative signals. Cell 1995; 80: 729–738
   PubMed Web of Science ®Google Scholar
• Kralovics R, Passamonti F, Buser AS, Teo S, Tiedt R, Passweg JR, Tichelli A, Cazzola M, Skoda RC. A gain-of-function mutation of JAK2 in myeloproliferative disorders. N Engl J Med 2005; 352: 1779–1790
   PubMed Web of Science ®Google Scholar
• Lacronique V, Boureux A, Valle V, Poirel H, Quang C, Mauchauffe M, Berthou C, Lessard M, Berger R, Ghysdael J, Bernard O. A TEL–JAK2 fusion protein with constitutive kinase activity in human leukemia. Science 1997; 278: 1309–1312
   PubMed Web of Science ®Google Scholar
• Levine RL, Wadleigh M, Cools J, Ebert BL, Wernig G, Huntly BJP, Boggon TJ, Wlodarska L, Clark JJ, Moore S, et al. Activating mutation in the tyrosine kinase JAK2 in polycythemia vera, essential thrombocythemia, and myeloid metaplasia with myelofibrosis. Cancer Cell 2005; 7: 387–397
   PubMed Web of Science ®Google Scholar
• Macchi P, Villa A, Giliani S, Sacco M, Frattini A, Porta F, Ugazio A, Johnston J, Candotti F, O'Shea J. Mutations of Jak-3 gene in patients with autosomal severe combined immune deficiency (SCID). Nature 1995; 377: 65–68
   PubMed Web of Science ®Google Scholar
• Muller M, Briscoe J, Laxton C, Guschin D, Ziemiecki A, Silvennoinen O, Harpur A, Barbieri G, Witthuhn B, Schindler C. The protein tyrosine kinase JAK1 complements defects in interferon-alpha/beta and -gamma signal transduction. Nature 1993; 366: 129–135
   PubMed Web of Science ®Google Scholar
• Neubauer H, Cumano A, Muller M, Wu H, Huffstadt U, Pfeffer K. Jak2 deficiency defines an essential developmental checkpoint in definitive hematopoiesis. Cell 1998; 93: 397–409
   PubMed Web of Science ®Google Scholar
• Okutani Y, Kitanaka A, Tanaka T, Kamano H, Ohnishi H, Kubota Y, Ishida T, Takahara J. Src directly tyrosine-phosphorylates STAT5 on its activation site and is involved in erythropoietin-induced signaling pathway. Oncogene 2001; 20: 6643–6650
   PubMed Web of Science ®Google Scholar
• Onishi M, Nosaka T, Misawa K, Mui AL, Gorman D, McMahon M, Miyajima A, Kitamura T. Identification and characterization of a constitutively active STAT5 mutant that promotes cell proliferation. Mol Cell Biol 1998; 18: 3871–3879
   PubMed Web of Science ®Google Scholar
• Parganas E, Wang D, Stravopodis D, Topham DJ, Marine JC, Teglund S, Vanin EF, Bodner S, Colamonici OR, van Deursen JM, et al. Jak2 is essential for signaling through a variety of cytokine receptors. Cell 1998; 93: 385–395
   PubMed Web of Science ®Google Scholar
• Pepper AE, Buckley RH, Small TN, Puck JM. Two mutational hotspots in the interleukin-2 receptor gamma chain gene causing human X-linked severe combined immunodeficiency. Am J Hum Genet 1995; 57: 564–571
   PubMed Web of Science ®Google Scholar
• Qing Y, Stark GR. Alternative Activation of STAT1 and STAT3 in Response to Interferon-γ. J Biol Chem 2004; 279: 41679–41685
   PubMed Web of Science ®Google Scholar
• Rane SG, Reddy EP. JAKs, STATs and Src kinases in hematopoiesis. Oncogene 2002; 21: 3334–3358
   PubMed Web of Science ®Google Scholar
• Roskoski R. Src protein-tyrosine kinase structure and regulation. Biochem Biophys Res Commun 2004; 324: 1155–1164
   PubMed Web of Science ®Google Scholar
• Russell S, Tayebi N, Nakajima H, Riedy M, Roberts J, Aman M, Migone T, Noguchi M, Markert M, Buckley R. Mutation of Jak3 in a patient with SCID: Essential role of Jak3 in lymphoid development. Science 1995; 270: 797–800
   PubMed Web of Science ®Google Scholar
• Saharinen P, Silvennoinen O. 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 2002; 277: 47954–47963
   PubMed Web of Science ®Google Scholar
• Saharinen P, Takaluoma K, Silvennoinen O. Regulation of the Jak2 tyrosine kinase by its pseudokinase domain. Mol Cell Biol 2000; 20: 3387–3395
   PubMed Web of Science ®Google Scholar
• Sasaki A, Yasukawa H, Shouda T, Kitamura T, Dikic I, Yoshimura A. CIS3/SOCS-3 suppresses erythropoietin (EPO) signaling by binding the EPO receptor and JAK2. J Biol Chem 2000; 275: 29338–29347
   PubMed Web of Science ®Google Scholar
• Schwaller J, Parganas E, Wang D, Cain D, Aster JC, Williams IR, Lee CK, Gerthner R, Kitamura T, Frantsve J, et al. Stat5 is essential for the myelo- and lymphoproliferative disease induced by TEL/JAK2. Mol Cell 2000; 6: 693–704
   PubMed Web of Science ®Google Scholar
• Silvennoinen O, Ihle J, Schlessinger J, Levy D. Interferon-induced nuclear signalling by Jak protein tyrosine kinases. Nature 1993; 366: 583–585
   PubMed Web of Science ®Google Scholar
• Smith A, Metcalf D, Nicola NA. Cytoplasmic domains of the common beta-chain of the GM-CSF/IL-3/IL-5 receptors that are required for inducing differentiation or clonal suppression in myeloid leukaemic cell lines. EMBO J 1997; 16: 451–464
   PubMed Web of Science ®Google Scholar
• Sokol L, Luhovy M, Guan Y, Prchal JF, Semenza GL, Prchal JT. Primary familial polycythemia: A frameshift mutation in the erythropoietin receptor gene and increased sensitivity of erythroid progenitor cells to erythropoietin. Blood 1995; 86: 15–22
   PubMed Web of Science ®Google Scholar
• Starr R, Willson TA, Viney EM, Murray LJ, Rayner JR, Jenkins BJ, Gonda TJ, Alexander WS, Metcalf D, Nicola NA, Hilton DJ. A family of cytokine-inducible inhibitors of signalling. Nature 1997; 387: 917–921
   PubMed Web of Science ®Google Scholar
• Thomis D, Gurniak C, Tivol E, Sharpe A, Berg L. Defects in B lymphocyte maturation and T lymphocyte activation in mice lacking Jak3. Science 1995; 270: 794–797
   PubMed Web of Science ®Google Scholar
• Tilbrook PA, Ingley E, Williams JH, Hibbs ML, Klinken SP. Lyn tyrosine kinase is essential for erythropoietin-induced differentiation of J2E erythroid cells. EMBO J 1997; 16: 1610–1619
   PubMed Web of Science ®Google Scholar
• Tilbrook PA, Palmer GA, Bittorf T, McCarthy DJ, Wright MJ, Sarna MK, Linnekin D, Cull VS, Williams JH, Ingley E, et al. Maturation of erythroid cells and erythroleumkemia development are affected by the kinase activity of Lyn. Cancer Res 2001; 61: 2453–2458
   PubMed Web of Science ®Google Scholar
• Ungureanu D, Saharinen P, Junttila I, Hilton DJ, Silvennoinen O. Regulation of Jak2 through the ubiquitin–proteasome pathway involves phosphorylation of Jak2 on Y1007 and interaction with SOCS-1. Mol Cell Biol 2002; 22: 3316–3326
   PubMed Web of Science ®Google Scholar
• Verma A, Kambhampati S, Parmar S, Platanias LC. Jak family of kinases in cancer. Cancer Metastasis Rev 2003; 22: 423–434
   PubMed Web of Science ®Google Scholar
• Weiss SR, Varmus HE, Bishop JM. The size and genetic composition of virus-specific RNAs in the cytoplasm of cells producing avian sarcoma-leukosis viruses. Cell 1977; 12: 983–992
   PubMed Web of Science ®Google Scholar
• Wilks A. Two putative protein-tyrosine kinases identified by application of the polymerase chain reaction. Proc Natl Acad Sci USA 1989; 86: 1603–1607
   PubMed Web of Science ®Google Scholar
• Witthuhn B, Quelle F, Silvennoinen O, Yi T, Tang B, Miura O, Ihle J. JAK2 associates with the erythropoietin receptor and is tyrosine phosphorylated and activated following stimulation with erythropoietin. Cell 1993; 74: 227–236
   PubMed Web of Science ®Google Scholar
• Wormald S, Hilton DJ. Inhibitors of cytokine signal transduction. J Biol Chem 2004; 279: 821–824
   PubMed Web of Science ®Google Scholar
• Wu H, Lui X, Jaenisch R, Lodish HF. Generation of committed erythroid BFU-E and CFU-E progenitors does not require erythropoietin or the erythropoietin receptor. Cell 1995; 83: 59–67
   PubMed Web of Science ®Google Scholar
• Xi S, Zhang Q, Dyer KF, Lerner EC, Smithgall TE, Gooding WE, Kamens J, Grandis JR. Src kinases mediate STAT growth pathways in squamous cell carcinoma of the head and neck. J Biol Chem 2003; 278: 31574–31583
   PubMed Web of Science ®Google Scholar
• Yamaoka K, Saharinen P, Pesu M, Holt V, Silvennoinen O, O'Shea J. The Janus kinases (Jaks). Genome Biol 2004; 5: 253
   PubMed Web of Science ®Google Scholar
• Yetter A, Uddin S, Krolewski JJ, Jiao H, Yi T, Platanias LC. Association of the interferon-dependent tyrosine kinase Tyk-2 with the hematopoietic cell phosphatase. J Biol Chem 1995; 270: 18179–18182
   PubMedGoogle Scholar
• Yu C-L, Meyer DJ, Campbell GS, Larner AC, Carter-Su C, Schwartz J, Jove R. Enhanced DNA-binding activity of a STAT3-related protein in cells transformed by the Src oncoprotein. Science 1995; 269: 81–83
   PubMed Web of Science ®Google Scholar
• Zhang JG, Farley A, Nicholson SE, Willson TA, Zugaro LM, Simpson RJ, Moritz RL, Cary D, Richardson R, Hausmann G, et al. The conserved SOCS box motif in suppressors of cytokine signaling binds to elongins B and C and may couple bound proteins to proteasomal degradation. Proc Natl Acad Sci USA 1999; 96: 2071–2076
   PubMed Web of Science ®Google Scholar
• Zhao RX, Xing S, Li Z, Fu XQ, Li QS, Krantz SB, Zhao ZHJ. Identification of an acquired JAK2 mutation in Polycythemia vera. J Biol Chem 2005; 280: 22788–22792
   PubMed Web of Science ®Google Scholar
• Zhou Y, Chen M, Cusack N, Kimmel L, Magnuson K, Boyd J, Lin W, Roberts J, Lengi A, Buckley R. Unexpected effects of FERM domain mutations on catalytic activity of Jak3: Structural implication for Janus kinases. Mol Cell 2001; 8: 959–969
   PubMed Web of Science ®Google Scholar