Src-related protein tyrosine kinases in hematopoiesis

Blood

Volumn 93, Issue 1, 1999, Pages 1-14

  Corey, Seth J ^a   Anderson, Steven M ^b  

^a CHILDREN S HOSPITAL OF PITTSBURGH   (United States)

^b NONE

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN TYROSINE KINASE;

CELL DIFFERENTIATION; CELL PROLIFERATION; DIMERIZATION; ENZYME ACTIVATION; ENZYME ACTIVITY; ENZYME CONFORMATION; HEMATOPOIESIS; HUMAN; NONHUMAN; PRIORITY JOURNAL; REVIEW; SIGNAL TRANSDUCTION;

EID: 0032931978     PISSN: 00064971     EISSN: None     Source Type: Journal    
DOI: 10.1182/blood.v93.1.1.401a45_1_14     Document Type: Review

References (165)

1. Metcalf D: The molecular control of cell division, differentiation, commitment, and maturation in haematopoietic cells. Nature 339:27, 1989
2. Uddin S, Fish EN, Sher D, Colamonici OR, Kellum M, Pith PMA, White MF, Platanias LC: The IRS-pathway operates distinctively from the State pathway in hematopoietic cells and transduces common and distinct signals during engagement of the insulin or interferon-alpha receptors. Blood 90:2574, 1997
3. Sherr CJ, Rettenmier CW, Sacca R, Roussel MF, Look AT, Stanley ER: The c-fms proto-oncogene is related to the receptor for the mononuclear phagocyte growth factor, CSF-1. Cell 41:665, 1985
4. Huang E, Nocka K, Beier DR, Chu T, Buck J, Lahm H, Wellner D, Leder P, Bessmer P: The hematopoieitic growth factor KL is encoded by the SI locus and is the ligand of the c-kit receptor, the gene product of the W locus. Cell 63:225, 1990
5. Anderson DM, Sherr CJ, Rettenmier CW, Lyman SD, Baird A, Wignall JM, Eisenman J, Rauch C, March CJ, Boswell HS, Girnpel SD, Cosman D, Williams DE: Molecular cloning of mast cell growth factor, a hematopoietin that is active in both membrane bound and soluble forms. Cell 63:235, 1990
6. Zsebo KM, Williams DA, Geissler EN, Broudy VC, Martin FN, Atkins HL, Hsu R, Birkett NC, Okino KH, Murdock DC, Jacobsen FW, Langlely KE, Smith KA,Takeishi T, Cattanach BM, Galli SJ, Suggs SV: Stem cell factor is encoded at the SI locus of the mouse and is the ligand for the c-kit tyrosine kinase receptor. Cell 63:213, 1990
7. Williams DE, Eisenman J, Baird A, Rauch C, Van Ness K, March CJ, Park LS, Martin U, Mochizuki DY, Boswell HS, Burgess GS, Cosman D, Lyman SD: Identification of a ligand for the c-kit proto-oncogene. Cell 63:167, 1990
8. Lyman SD, James L, Vanden Bos T, de Vries P, Brasel K, Gliniak B, Hollingworth LT, Picha KS, McKenna HJ, Splett RR, Fletcher FA, Maraskovsky E, Farrah T, Foxworthe D, Williams DE, Beckmann MP: Molecular cloning of a ligand for the flt3/flk2 tyrosine kinase receptor: A proliferative factor for primative hematopoietic cells. Cell 75:1157, 1993
9. Kaczarski RS, Mufti GJ: The cytokine receptor superfamily. Blood Rev 5:193, 1991
10. Bagley CJ, Woodcock JM, Stomski FC, Lopez AF: The structural and functional basis of cytokine activation: Lessons from the common β subunit of the granulocyte-macrophage colony-stimulating factor, interleukin-3 (IL-3), and IL-5 receptors. Blood 89:1471, 1997
11. Avalos BR: Molecular analysis of the granulocyte colony-stimulating factor receptor. Blood 88:761, 1996
12. Argetsinger LS, Campbell GS, Yang X, Witthuhn BA, Silvennoinen O, Ihle JN, Carter-Su C. Identification of JAK2 as a growth hormone receptor-associated tyrosine kinase. Cell 74:237, 1993
13. Silvennoinen O, Witthuhn BA, Quelle FW, Cleveland JL, Yi T, Ihle JN. Structure of the murine Jak2 protein-tyrosine kinase and its role in interleukin 3 signal transduction. Proc Natl Acad Sci USA 90:8429, 1993
14. Witthuhn BA, Quelle FW, Silvennoinen O, Yi T, Tang B, Miura O, Ihle JN: JAK2 associates with the erythropoietin receptor and is tyrosine phosphorylated and activated following stimulation with erythropoietin. Cell 74:227, 1993
15. Stahl N, Boulton TG, Farruggella T, Ip NY, Davis S, Witthuhn BA, Quelle FW, Silvennoinen O, Barbieri G, Pellegrini S, Ihle JN, Yancopoulos GD: Association and activation of Jak-Tyk kinases by CNTF-LIF-OSM-IL-6 B receptor components. Science 263:92, 1994
16. Ihle JN, Witthuhn BA, Quelle FW, Yamamoto K, Thierfelder WE, Kreider BL, Silvennoinen O: Signaling by the cytokine receptor superfamily. Trends Biochem Sci 19:222, 1994
17. Anderson SM, Jorgensen B: Activation of src-related tyrosine kinases by IL-3. J Immunol 155:1660, 1995
18. Torigoe T, O'Connor R, Santoli D, Reed JC: Interleukin-3 regulates the activity of the LYN protein-tyrosine kinase in myeloid-committed leukemic cell lines. Blood 80:617, 1992
19. Corey S, Eguinoa A, Puyana-Theall K, Bolen JB, Cantley L, Mollinedo F, Jackson TR, Hawkins PT, Stephens LR: Granulocyte macrophage-colony stimulating factor stimulates both association and activation of phosphoinositide 30H-kinase and src-related tyrosine kinase(s) in human myeloid derived cells. EMBO J 12:2681, 1993
20. English BK, Ihle JN, Myracle A, Yi T: Hck tyrosine kinase activity modulates tumor necrosis factor production by murine macrophages. J Exp Med 178:1017, 1993
21. Ernst M, Gearing DP, Dunn AR: Functional and biochemical association of hck with the LIF/IL-6 receptor signal transducing subunit gp130 in embryonic stem cells. EMBO J 13:1574, 1994
22. Appleby MW, Kemer JD, Chien S, Maliszewski C, Bondadaa S, Perlmutter RM: Involvement of p59fynT in interleukin-5 receptor signaling. J Exp Med 182:811, 1995
23. Pazdrak K, Schreiber D, Forsythe P, Justement L, Alam R: The intracellular signal transduction mechanism of interleukin 5 in eosinophils: The involvement of lyn tyrosine kinase and the ras-raf-1 -MEK-microtubule-associated protein kinase pathway. J Exp Med 181:1827, 1995
24. Corey SJ, Burkhardt AL, Bolen JB, Geahlen RL, Tkatch LS, Tweardy DJ: Granulocyte colony-stimulating factor receptor signaling involves the formation of a three component complex with lyn and syk protein-tyrosine kinases. Proc Natl Acad Sci USA 91:4683, 1994
25. Clevenger CV, Medaglia MV: The protein tyrosine kinase P59fyn is associated with prolactin (PRL) receptor and is activated by PRL stimulation of T-lymphocytes. Mol Endocrinol 8:674, 1994
26. Saharinen P, Ekman N, Sarvas K, Parker P, Alitalo K, Silvennoinen O: The Bmx tyosine kinase induces activation of the stat signaling pathway, which is specifically inhibited by protein kinase cδ. Blood 90:4341, 1997
27. Weil D, Power M-A, Smith SI, Li CL: Predominant expression of murine Bmx tyrosine kinase in the granulo-monocytic lineage. Blood 90:4332, 1997
28. Russell SM, Tayebi N, Nakajima H, Riedy MC, Ropberts JL, Aman MJ, Migone T-S, Noguchi M, Markert ML, Buckley RH, O'Shea JJ, Leonard WJ: Mutation of Jak3 in a patient with SCID: essential role of Jak3 in lymphoid development. Science 270:797, 1995
29. Villa A, Sironi M, Macchi P, Matteucci C, Notarangelo LD, Vezzoni P, Mantovani A: Monocyte function in a severe combined immunodeficient patient with a donor splice mutation in the Jak3 gene. Blood 88:817, 1996
30. Neubauer H, Cumano A, Muller M, Wu H, Huffstadt U, Pfeffer K: Jak2 deficiency defines an essential developmental checkpoint in definitive hematopoiesis. Cell 93:397, 1998
31. Parganas E, Wang D, Stravopodis D, Topham DJ, Marine J-C, Teglund S, Vanin EF, Bodner S, Colamonici OR, van Deursen JM, Grosveld G, Ihle JN: Jak2 is essential for signaling through a variety of cytokine receptors. Cell 93:385, 1998
32. Rodif SJ, Meraz MA, White JM, Lampe PA, Riley JK, Arthur CD, King KL, Sheehan KCF, Yin L, Oennica D, Johnson EM Jr, Schreiber RD: Disruption of the Jak1 gene demonstrates obligatory and nonredundant roles of the Jaks in cytokine-induced biological responses. Cell 93:373, 1998
33. Chan AC, Desai DM, Weiss A: The role of protein tyrosine kinases and protein tyrosine phosphatases in T cell antigen receptor signal transduction. Annu Rev Immunol 12:555, 1994
34. Cambier JC, Pleiman CM, Clark M: Signal transduction by the B cell antigen receptor and its coreceptors. Annu Rev Immunol 12:457, 1994
35. Cantrell D: T cell antigen receptor signal transduction pathways. Annu Rev Immunol 14:259, 1996
36. Cheng AM, Chan AC: Protein tyrosine kinases in thymocyte development. Curr Opin Immunol 9:525, 1997
37. Kurosaki T: Molecular Mechanisms in B cell antigen receptor signaling. Curr Opin Immunol 9:309, 1997
38. Jouvin MH, Numerof RP, Kinet JP: Signal transduction through the conserved motifs of the high affinity IgE receptor FcE RI. Semin Immunol 7:29, 1995
39. Kawakami Y, Furue M, Kawakami T: Identification of fyn-encoded proteins in normal human blood cells. Oncogene 4:389, 1989
40. Davidson D, Chow LML, Foumel M, Veillette A: Differential regulation of T cell antigen responsiveness by isoforms of the src-related tyrosine protein kinase p59fyn. J Exp Med 175:1483, 1992
41. Yi T, Bolen JB, Ihle JN: Hematopoietic cells express two forms of lyn kinase differing by 21 amino acids in the amino acids. Mol Cell Biol 11:2391, 1992
42. Levy JB, Dorai T, Wang L-H, Brugge JS: The structurally distinct form of pp60c-src detected in neuronal cells is encoded by a unique c-src mRNA. Mol Cell Biol 7:4142, 1987
43. Matrinez R, Mathey-Prevot B, Bemards A, Baltimore D: Neuronal pp60c-src contains a six amino acid insertion relative to its non-neuronal counterpart. Science 237:411, 1998
44. Lock P, Ralph S, Stanley E, Boulet I, Ramsay R, Dunn AR: Two isoforms of murine hck, generated by utilization of alternative translational initiation codons, exhibit different patterns of subcellular localization. Mol Cell Biol 15:43-63, 1995
45. Xu W, Harrison SC, Eck MJ: Three-dimensional structure of the tyrosine kinase c-src. Nature 385:595, 1997
46. Sicheri F, Moarefi I, Kuriyan J: Crystal structure of the src family tyrosine kinase hck. Nature 385:602, 1997
47. Golden A, Brugge JS: The src oncogene, in Reddy EP, Skalka AM, Curran T (eds): The Oncogene Handbook. New York, NY, Elsevier, 1988, p 149
48. Zhao YH, Baker H, Walaas SI, Sudol M: Localization of p62c-yes protein in mammalian neural tissues. Oncogene 6:1725, 1991
49. Kruger J, Zhao YH, Murphy D, Sudol M: Differential expression of p62c-yes in normal, hyperplastic and neoplstic human epidermis. Oncogene 6:933, 1991
50. Zhao YH, Krueger JG, Sudol M: Expression of cellular-yes protein in mammalian tissues. Oncogene 5:1629, 1990
51. Willman CL, Stewrat CC, Longacre TL, Head DR, Habbersett R, Ziegler SF, Perlmutter RM: Expression of the c-fgr and hck protein-tyrosine kinases in acute myeloid leukemic blasts is associated with early commitment and differentiation events in the monocytic and granulocytic lineages. Blood 77:726, 1991
52. Grant SGN, O'Dell TJ, Karl KA, Stein PL, Soriano P, Kandel ER: Impaired long-term potentiation, spatial learning, and hippocampal development in fyn mutant mice. Science 258:1903, 1992
53. Soriano P, Montgomery C, Geske R, Bradley A: Targeted disruption of the c-src proto-oncogene leads to osteopetrosis in mice. Cell 64:693, 1991
54. Veillette A, Bookman MA, Horak EM, Samelson LE, Bolen JB: Signal transduction through the CD4 receptor involves the activation of the internal membrane tyrosine-protein kinase p561ck. Nature 338:257, 1990
55. Lou K, Sefton BM: Cross-linking of T-cell surface molecules CD4 and CD8 stimulates phosphorylation of the Ick tyrosine protein kinase at the autophosphorylation site. Mol Cell Biol 10:5305, 1990
56. Veillette A, Bolen JB, Bookman MA: Alterations in tyrosine protein phosphorylation induced by antibody-mediated cross-linking of the CD4 receptor of T lymphocytes. Mol Cell Biol 10:4441, 1990
57. Yamanashi Y, Fukushige S, Semba K, Sukegawa J, Miyajima N, Matsubara K, Yamamoto T, Toyshima K: The yes-related cellular gene lyn encodes a possible tyrosine kinase similar to p561ck. Mol Cell Biol 7:237, 1987
58. Yamanashi Y, Mori S, Yoshida M, Kishimoto T, Inoue K, Yamamoto T, Toyoshima K: Selective expression of a protein-tyrosine kinase, p561yn, in hematopoietic cells and association with production of human T-cell lymphotropic virus type 1. Proc Natl Acad Sci USA 86:6538, 1989
59. Holtzman DA, Cook WD, Dunn AR: Isolation and sequence of a cDNA corresponding to a src-related gene expressed in murine hematopoietic cells. Proc Natl Acad Sci USA 84:8325, 1987
60. Quintrell N, Lebo R, Varmus H, Bishop JM, Pettenati MJ, LeBeau MM, Diaz MO, Rowley JD: Identification of a human gene (HCK) that encodes a protein tyrosine kinase and is expressed in hematopoietic cells. Mol Cell Biol 7:2267, 1987
61. Dymecki SM, Niederhuber JE, Desiderio SV: Specific expression of a tyrosine kinase gene blk in B lymphoid cells. Science 247:332, 1992
62. Hanks SK, Quinn AM, Hunter T: The protein kinase family: Conserved features and deduced phylogeny of the catalytic domains. Science 241:42, 1988
63. Songyang Z, Shoelson SE, Chaudhuri M, Gish G, Pawson T, Haser WG, King F, Roberts T, Ratnofsky S, Lechleider RJ, Neel BG, Birge RB, Fajardo JE, Chou MM, Hanafasa H, Schaffhausen B, Cantley LC: SH2 domains recognize specific phosphopeptide sequences. Cell 72:767, 1993
64. Songyang Z, Shoelson SE, McGlade J, Olivier P, Pawson T, Bustelo XR, Barbacid M, Sabe H, Hanafusa H, Yi T, Ren R, Baltimore D, Patnofsky S, Feldman RA, Cantley LC: Specific motifs recognized by the SH2 domains of csk, 3BP2, fps/fes, GRB-2, HCP, SHC, syk, and vav. Mol Cell Biol 14:2777, 1994
65. Cohen GB, Ren R, Baltimore D: Modular binding domains in signal transduction proteins. Cell 80:237, 1995
66. Ren R, Mayer BJ, Cicchetti P, Baltimore D: Identification of a ten-amino acid proline-rich SH3 binding site. Science 259:1157, 1993
67. Mayer BJ, Eck MJ: SH3 domains. Minding your p's and q's. Curr Biol 5:364, 1995
68. Turner JM, Brodsky MH, Irving BA, Levin SD, Perlmutter RM, Littman DR: Interaction of the unique-terminal region of tyrosine kinase p561ck with cytoplasmic domains of CD4 and CD8 is mediated by cysteine motifs. Cell 60:755, 1990
69. Pleiman CM, Abrams C, Gauen LT, Bedzyk W, Jongstra J, Shaw AS, Cambier JC: Distinct p53/p56 lyn and P59fyn domains associate with nonphosphorylated and phosphorylated Igα. Proc Natl Acad Sci USA 91:4268, 1994
70. Alland L, Peseckis SM, Atherton RE, Berthiaume L, Resh MD: Dual myristylation and palmitylation of src family member p59fyn affects subcellular localization. J Biol Chem 269:16701, 1994
71. Sigal CT, Zhou W, Buser CA, Mclaughlin S, Resh MD: Amino-terminal basic residues of src mediate membrane binding through electrostatic interaction with acidic phospholipids. Proc Natl Acad Sci USA 91:12253, 1994
72. Cooper JA, Gould KL, Cartwright CA, Hunter T: Tyr527 is phosphorylated in pp60src: Implication for regulation. Science 231: 1431, 1986
73. Cooper JA, King CS: Dephosphorylation or antibody binding to the carboxy terminus stimulates pp60c-src. Mol Cell Biol 6:4467, 1986
74. Okada M, Nakagawa H: A protein tyrosine kinase involved in regulation of pp60src function. J Biol Chem 264:20886, 1989
75. Sabe H, Knudsen B, Okada M, Nada S, Nakagawa H, Hanafusa H: Molecular cloning and expression of chicken C-terminal src kinase: lack of stable association with c-src protein. Proc Natl Acad Sci USA 89:2190, 1992
76. Superti-Furga G, Fumagalli S, Koegl M, Courtneidge SA, Dreatta G: Csk inhibition of c-src activity requires both the SH2 and SH3 domains of src. EMBO J 12:2625, 1993
77. Sieh M, Bolen JB, Weiss A: CD45 specifically modulates binding of lck to a phosphopeptide encompassing the negative regulatory tyrosine of lck. EMBO J 12:315, 1993
78. Mustelin T, Coggeshall KM, Altman A: Rapid activation of the T-cell tyrosine protein kinase pp56 lck by the CD45 phosphotyrosine phosphatase. Proc Natl Acad Sci USA 86:6302, 1989
79. Ostergaard HL, Trowbridge IS: Coclustering CD45 with CD4 or CD8 alters the phosphorylation and lck kinase activity of p56. J Exp Med 172:347, 1990
80. Mustelin T, Altman A: Dephosphorylation and activation of the T cell tyrosine kinase pp56 lck by the leukocyte comon antigen (CD45). Oncogene 5:809, 1990
81. Kmiecik TE, Shalloway D: Activation and suppression of pp60c-src transformation ability by mutation of its primary sites of tyrosine phosphorylation. Cell 49:65, 1987
82. Piwnica-Worms H, Saunders KB, Roberts TM, Smith AE, Cheng SH: Tyrosine phosphorylation regualtes the biochemical and biological properties of pp60c-src. Cell 49:75, 1987
83. Reynolds AB, Vila J, Lansing TJ, Potts WM, Weber MJ, Parsons JT: Activation of the oncogenic potential of the avain cellular src protein by specific alteration of the carboxy terminus. EMBO J 6:2359, 1987
84. Moarefi I, LaFevre-Bemt M, Sicheri F, Huse M, Lee C-H, Kuriyan J, Miller WT: Activation of the src-family tyrosine kinase hck by SH3 domain displacement. Nature 385:650, 1997
85. Courtneidge SA, Dhand R, Pilat D, Twamley GM, Waterfield MD, Roussel MF: Activation of src family kinases by colony-stimulating factor-1, and their association with its receptor. EMBO J 12:943, 1993
86. Twamley-Stein GM, Pepperkok R, Ansorge W, Courtneidge SA: The src family tyrosine kinases are required for platelet-derived growth factor-mediated signal transduction in NIH 3T3 cells. Proc Natl Acad Sci USA 90:7696, 1993
87. Roche S, Koegel M, Barone MV, Roussel MF, Courtneidge SA: DNA synthesis induced by some but not all growth factors requires src family protein kinases. Mol Cell Biol 15:1102, 1995
88. Landgren E, Blume-Jensen P, Courtneidge SA, Claesson-Welsh L: Fibroblast growth factor receptor-1 regulation of src family kinases. Oncogene 10:2027, 1995
89. Alonso G, Koegl M, Mazurenko N, Courtneidge SA: Sequence requirements for binding of src family tyrosine kinases to activated growth factor receptors. J Biol Chem 270:9840, 1995
90. Linnekin D, DeBerry CS, Mou S: Lyn associates with the juxtamembrane region of c-Kit and is activated by stem cell factor in hematopoietic cell lines and normal progenitor cells. J Biol Chem 272:27450, 1997
91. Corey SJ, Dombrosky-Ferlan PM, Zuo S, Krohn E, Donnenberg AD, Zorich P, Romero G, Takata M, Kurosaki T: Requirement of src kinase lyn for induction of DNA synthesis by granulocyte colony-stimulating factor. J Biol Chem 273:3230, 1998
92. Barone MV, Courtneidge SA: Myc but not fos rescue of PDGF signalling block caused by kinase-inactive src. Nature 378:509, 1995
93. Roche SI, Fumagalli S, Courtneidge SA: Requirement for src family protein tyrosine kinases in G2 for fibroblast cell division. Science 269:1567, 1995
94. Pathan NI, Geahlen RL, Harrison ML: The protein tyrosine kinase Lck associates with and is phosphorylated by Cdc2. J Biol Chem 271:27517, 1996
95. Kharbanda S, Saleem A, Yuan ZM, Kraeft S, Weischelbaum R, Chen LB, Kufe D: Nuclear signaling induced by ionizing radiation involves colocalization of the activated p56/p53lyn tyrosine kinase with p34cdc2. Cancer Res 56:3617, 1996
96. Uckun FM, Tuel-Ahlgren L, Waddick KG, Jun X, Jin J, Myers DE, Rowley RB, Burkhardt AL, Bolen JB: Physical and functional interactions between Lyn and p34cdc2 kinases in irradiated human B-cell precursors. J Biol Chem 271:6389, 1996
97. Imamoto A, Soriano P: Disruption of the csk gene, encoding a negative regulator of src family tyrosine kinases, leads to neural tube defects and embryonic lethality. Cell 73:1117, 1995
98. Lowell CA, Soriano PI, Varmus HE: Functional overlap in the src family: Inactivation of hck and fgr impairs natural immunity. Genes Dev 8:387, 1994
99. Lowell CA, Niwa M, Soriano P, Varmus H: Deficiency of the Hck and Src Tyrosine kinases results in extreme levels of extramedullary hematopoiesis. Blood 87:1780, 1996
100. Stein PL, Vogel H, Soriano P: Combined deficiencies of Src, Fyn, and Yes tyrosine kinases in mutant mice. Genes Dev 8:1999, 1994
101. Lowe C, Yoneda T, Boyce BF, Chen H, Mundy GR, Soriano P: Osteopetrosis in src-deficient mice is due to an autonomous defect of osteoclasts. Proc Natl Acad Sci USA 90:4485, 1993
102. Boyce BF, Yoneda T, Lowe C, Soriano P, Mundy GR: Requirement of pp60c-src expression for osteoclasts to form ruffled borders and resorb bone in mice. J Clin Invest 90:1622, 1992
103. Schwartzberg PL, Xing LP, Hoffmann O, Lowell CA, Garrett L, Boyce BF, Varmus HE: Rescue of osteoclast function by transgenic expression of kinase deficient src in src-/-mutant mice. Genes Dev 11:2835, 1997
104. Wiktor-Jedrzejcak W, Urbanowska E, Aukerman SL, Pollard JW, Stanley ER, Ralph P, Ansari AA, Sell KW, Szperl M: Correction by CSF-1 of defects in the osteopetrotic op/op mouse suggests local, developmental, and humoral requirements for this growth factor. Exp Hematol 19:1049, 1991
105. Molina TJ, Bachmann MF, Kundig TM, Zinkemagel RM, Mak TW: Peripheral T cells in mice lacking p56lck do not express significant antiviral effector functions. J Immunol 151:699, 1993
106. Stein PL, Lee H, Rich S, Soriano P: pp59fyn mutant mice display differential signalling in thymocytes and peripheral T cells. Cell 70:741, 1992
107. 106a. 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 83:301, 1995
108. 106b. Nishizumi H, Taniuchi I, Yamanashi Y, Kitamura D, Ilic D, Mori S, Watanabe T, Yamamoto T: Impaired proliferation of peripheral B cells and indication of autoimmune disease in lyn-deficient mice. Immunity 3:549, 1995
109. Lowell CA, Fumagalli L, Berton G: Deficiency of Src family kinases p59/61hck and p58c-fgr results in defective adhesion-dependent neutrophil functions. J Cell Biol 133:895, 1996
110. De Franceschi L, Fumagalli L, Olivieri O, Corrocher R, Lowell CA, Berton G: Deficiency of src family kinases Fgr and Hck results in activation of erythrocyte K/Cl cotransport. J Clin Invest 99:220, 1997
111. Hunter T, Sefton BM: Transforming gene product of Rous sarcoma virus phosphorylates tyrosine. Proc Natl Acad Sci USA 77:1311, 1980
112. Sefton BM, Hunter T, Raschke WC: Evidence that the Abelson virus protein functions in vivo as a protein kinase that phosphroylates tyrosine. Proc Natl Acad Sci USA 78:1552, 1981
113. Cooper JA, Hunter T: Changes in protein phosphorylation in Rous sarcome virus-transformed chicken embryo cells. Mol Cell Biol 1:165, 1981
114. Zhou S, Carraway KL III, Eck MJ, Harrison SC, Feldman RA, Mohammadi M, Schlessinger J, Hubbard SR, Smith DP, Eng C: Catalytic specificity of protein-tyrosine kinases is critical for selective signalling. Nature 373:536, 1995
115. Sparks AB, Rider JE, Hoffman NG, Fowlkes DM, Quilliam LA, Kay BK: Distinct ligand preferences of src homology 3 domains from src, yes, abl, cortactin, p53bp2, PLCγ, crk and grb2. Proc Natl Acad Sci USA 93:1540, 1996
116. Rickles RJ, Botfield MC, Weng Z, Taylor JA, Green OM, Brugge JS, Zoller MJ: Identification of src, fyn, lyn, P13K and abl SH3 domain ligands using phage display libraries. EMBO J 13:5598, 1994
117. Rickles RJ, Botfield MC, Zhou X-M, Hanery PA, Brugge JS, Zoller MJ: Phage display selections of ligand residues important for src homology 3 domain binding specificity. Proc Natl Acad Sci USA 92:10909, 1995
118. Sparks AB, Quilliam LA, Thom JM, Der CJ, Kay BK: Identification and characterization of src SH3 ligands from phage-displayed random peptide libraries. J Biol Chem 269:23853, 1994
119. Cheadle C, Ivashchenko Y, South V, Searfoss GH, French S, Howk R, Ricca GA, Jaye M: Identification of a src SH3 domain binding motif by screening a random phage display library. J Biol Chem 269:24034, 1994
120. Yu H, Chen JK, Feng S, Dalgamo DC, Brauer AW, Schreiber SL: Structural basis for the binding of proline-rich peptides to SH3 domains. Cell 76:933, 1994
121. Erwin JL, Anderson SM: Analysis of phosphotyrosine-containing proteins present in v-src-infected myeloid progenitor cells. Oncogene 7:1101, 1992
122. Nagai K, Takata H, Kurosaki T: Tyrosine phosphorylation of Shc is mediated through Lyn and Syk in B cell receptor signaling. J Biol Chem 270:6824, 1995
123. Ptasznik R, Traynor-Kaplan A, Bokoch GM: G protein-coupled chemoattractant receptors regulate Lyn tyrosine kinase Shc adapter protein signaling complexes. J Biol Chem 270:19969, 1995
124. Li B, Subleski M, Fusaki N, Yamamoto T, Copeland T, Princler GL, Rung H, Kamata T: Catalytic activity of the mouse guanine nucleotide exchanger mSOS is activated by Fyn tyrosine protein kinase and the T cell antigen receptor in T cells. Proc Natl Acad Sci USA 93:1001, 1996
125. Datta SR, Dudek H, Tao X, Masters S, Fu H, Gotoh Y, Greenberg ME: Akt phosphorylation of BAD couples survival signals to the cell-intrinsic death machinery. Cell 91:231, 1997
126. Mano H, Yamashita Y, Miyazato A, Miura Y, Ozawa K: Tec protein-tyrosine kinase is an effector molecule of Lyn protein-tyrosine kinase. FASEB J 10:637, 1996
127. Takhashi-Tezuka M, Hibi M, Fujitani Y, Fukada T, Yamaguichi T, Hirano T: Tec tyrosine kinase links the cytokine receptors to PI 3-kinase probably through Jak. Oncogene 14:2273, 1997
128. Schaller MD, Borgman CA, Cobb BS, Vines RR, Reynolds AB, Parsons JT: pp125FAK, a structurally distinctive protein-tyrosine kinase associated with focal adhesions. Proc Natl Acad Sci USA 89:5192, 1992
129. Burridge K, Turner CE, Romer LH: Tyrosine phosphorylation of paxillin and pp125FAK accompanies adhesion to extracellular matrix: A role in cytoskeletal assembly. J Cell Biol 119:8939, 1992
130. Cobb BS, Schaller MD, Leu T-H, Parsons JT: Stable association of pp60src and p59fyn with the focal adhesion-associated protein kinase, pp 125 FAK. Mol Cell Biol 14:147, 1994
131. Schaller MD, Hildebrand JD, Shannon JD, Fox JW, Vines RR, Parsons JT: Autophosphorylation of the focal adhesion kinase, pp125FAK, directs SH2-dependent binding of pp60src. Mol Cell Biol 14:1680, 1994
132. Chen H-C, Appeddu PA, Isoda H, Guan J-L: Phosphorylation of tyrosine 397 in focal adhesion kinase is required for binding of phosphatidylinositol 3-kinase. J Biol Chem 271:26329, 1996
133. Thomas SM, Soriano P, Imamoto A: Specific and redundant roles of Src and Fyn in organising the cytoskeleton. Nature 376:267, 1995
134. Schlaepfer DD, Hanks SK, Hunter T, van der Geer P: Integrin-mediated signal transduction linked to ras pathway by GRB2 binding to focal adhesion kinase. Nature 372:786, 1994
135. Schlaepfer DD, Hunter T: Focal adhesion kinase overexpression enhances ras-dependent integrin signaling to ERK2/mitogen-activated protein kinase through interactions with and activation or c-src. J Biol Chem 272:13189, 1997
136. Tycko B, Smith SD, Sklar J: Chromosomal translocations joining LCK and TCRB loci in human T cell leukemia. J Exp Med 174:867, 1991
137. Vetrie D, Vorechovsky I, Sideras P, Holland J, Davies A, Flinter F, Hammarstrom L, Kinnon C, Levinsky R, Babrow M, Edvard Smith CI, Bentley DR: The gene involved in X-linked agammaglobulinaemia is a member of the src family of protein-tyrosine kinase. Nature 361:226, 1993
138. Arpaia E, Shahar M, Dadi H, Cohen A, Roifinan CM: Defective T cell receptor signaling and CD8+ thymic selection in humans lacking Zap-70 kinase. Cell 76:947, 1994
139. Elder ME, Lin D, Clever J, Chan AC, Hope TJ, Weiss A, Parslow TG: Human severe combined immunodeficienct due to a defect in ZAP-70, a T cell tyrosine kinase. Science 264:1596, 1994
140. Chan AC, Kadlecek TA, Elder ME, Filipovich AH, Kuo W-L, Iwashima M, Parslow TG, Weiss A: ZAP-70 deficiency in an autosomal recessive form of severe combined immunodeficiency. Science 264: 1599, 1994
141. Uckun FM, Evans WE, Forsyth CJ, Waddick KG, Ahlgren LT, Chelstrom LM, Burkhardt A, Bolen J, Myers DE: Biotherapy of B cell precursor leukemia by targeting genistein to CD19-associated tyrosine kinases. Science 267:886, 1995
142. Burton EA, Hunter S, Wu SC, Anderson SM: Binding of src-like kinases to the β subunit of the interleukin-3 receptor. J Biol Chem 272:16189, 1997
143. Tortolani PJ, Lal BK, Riva A, Johnson JA, Chen Y-Q, Reamon GH, Beckwith M, Longo D, Ortaldo JR, Bhatia K, McGrath I, Kehrl JH, Tuscano J, McVicar DW, O'Shea JJ: Regulation of JAK3 expression and activation in human B cells and B cell malignancies. J Immunol 155:5220, 1995
144. Peeters P, Raynaud SD, Cools J, Wlodarska I, Grosgeorge J, Philip P, Manpoux F, Van Rompaey L, Baens M, Van den Berghe H, Maryman P: Fusion of TEL, the ETS-varient 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 90:2535, 1997
145. Lacronique V, Boureux A, Valle VD, Poirel H, Quang CT, Mauchauffe M, Berthou C, Lessard M, Berger R, Ghysdael J, Bernard OA: A TEL-JAK2 fusion protein with constitutive kinase activity in human leukemia. Science 278:1309, 1997
146. Rui H, Kirken RA, Farrar WL: Activation of receptor-associated tyrosine kinase JAK2 by prolactin. J Biol Chem 269:5364, 1994
147. Lebrun J-J, Ali S, Sofer L, Ulrich A, Kelly PA: Prolactin-induced proliferation of Nb2 cells involves tyrosine phosphorylation of the prolactin receptor and its associated tyrosine kinase JAK2. J Biol Chem 269:14021, 1994
148. Watanabe S, Itoh T, Arai K: 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, 1996
149. Watling D, Guschin D, Muller M, Silvennoinen O, Witthuhn BA, Quelle FW, Rogers NC, Schinder C, Stark GR, Kerr IM: Complementation by the protein tyrosine kinase JAK2 of a mutant cell line defective in the interferon-γ signal transduction pathway. Nature 366:166, 1993
150. Muller M, Briscoe J, Laxton C, Guschin D, Ziemiecki A, Silvennoinen O, Harpur AG, Barbieri G, Witthuhn BA, Schindler C, Pellegrini S, Wilks AF, Ihle JN, Stark GR, Kerr IM: The protein tyrosine kinase JAK1 complements defects in interferon-α/β and -γ signal transduction. Nature 366:129, 1993
151. Shimoda K, Feng J, Murakami H, Nagata S, Watling D, Rogers NC, Stark GR, Kerr IM, Ihle JN: Jak1 plays an essential role for receptor phosphorylation and Stat activation in response to granulocyle colony-stimulating factor. Blood 90:597, 1997
152. Takata M, Sabe H, Hata A, Inazu T, Homma Y, Nukada T, Yamamura H, Kurosaki T: Tyrosine kinases Lyn and Syk regulate B cell receptor-coupled Ca2+ mobilization through distinct pathways. EMBO J 13:1341, 1994
153. Dorsch M, Fan PD, Danial NN, Rothman PB, Goff SP: The thrombopoietin receptor can mediate proliferation without activation of the Jak-STAT pathway. J Exp Med 186:1947, 1997
154. Chaturvedi P, Reddy MVR, Reddy EP: Src kinases and not JAKs activate STATs during IL-3 induced myeloid cell proliferation. Oncogene 16:1749, 1998
155. Tilbrook PA, Ingley E, Williams JH, Hibbs ML, Klinken SP: Lyn tyrosine kinase is essential for eythropoietin-induced differentiation of J2E cells. EMBO J 16:1610, 1997
156. Yu CL, Meyer DJ, Campbell GS, Larner AC, Carter-Su C, Schwartz J, Jove R: Enhanced DNA-binding activity of Stat3-related protein in cells transformed by the Src oncoprotein. Science 269:81, 1995
157. Yu CL, Jove R, Burakoff SR: Constitutive activation of the Janus kinase-STAT pathway in T lymphoma overexpressing the Lck protein tyrosine kinase. J Immunol 159:5206, 1997
158. Turkson J, Bowman T, Garcia R, Caldenhoven E, DeGroot RP, Jove R: Stat3 activation by Src induces specific gene regulation and is required for cell transformation. Mol Cell Biol 18:2545, 1998
159. Chin H, Arai A, Wakao H, Kamiyama R, Miyasaka N, Miura O: Lyn physically associates with the erythropoieitin and may play a role in activation of the StatS pathway. Blood 91:3734, 1998
160. Feng J, Witthuhn BA, Matsuda T, Kouber F, Kerr IM, Ihle JN: Activation of Jak2 catalytic activity requires phosphorylation of Y1007 in the kinase activation loop. Mol Cell Biol 17:2497, 1997
161. Quelle FW, Sato N, Witthuhn BA, Inhom RC, Eder M, Miyajima A, Griffin JD, Ihle JN: JAK2 associates with the βc chain of the receptor for granulocyte-macrophage colony-stimulating factor, and its activation requires the membrane-proximal region. Mol Cell Biol 14:4335, 1994
162. Nakamura N, Chin H, Miyasaka N, Miura O: An epidermal growth factor receptor/Jak2 tyrosine kinase domain chimera induces tyrosine phosphorylation of StatS and transduces a growth signal in hematopoietic cells. J Biol Chem 271:19483, 1996
163. Hubbard SR, Wei L, Ellis L, Hendrickson WE: Crystal structure of the tyrosine kinase domain of the human insulin receptor. Nature 372:746, 1994
164. Hubbard SR, Mohammadi M, Schlessinger J: Autoregulatory mechanisms in protein-tyrosine kinases. J Biol Chem 273:11987, 1998
165. Golub TR, Goga A, Barker GF, Afar DE, McLaughlin J, Bohlander SK, Rowley JD, Witte ON, Gilliland DG: Oligomerization of the ABL tyrosine kinase by the ETS protein TEL in human leukemia. Mol Cell Biol 16:4107, 1996