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Role of ABL family kinases in cancer: from leukaemia to solid tumours

Greuber, Emileigh K., Smith-Pearson, Pameeka, Wang, Jun, Pendergast, Ann Marie·2013·Nature Reviews Cancer

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  1. Goff, S. P., Gilboa, E., Witte, O. N. & Baltimore, D. Structure of the Abelson murine leukemia virus genome and the homologous cellular gene: studies with cloned viral DNA. Cell 22, 777–785 (1980). · DOI
  2. Ben-Neriah, Y., Daley, G. Q., Mes-Masson, A. M., Witte, O. N. & Baltimore, D. The chronic myelogenous leukemia-specific P210 protein is the product of the bcr/abl hybrid gene. Science 233, 212–214 (1986). References 1 and 2 are historic manuscripts that describe the identification of normal and oncogenic forms of mouse and human ABL kinases. · DOI
  3. Lin, J. & Arlinghaus, R. Activated c-Abl tyrosine kinase in malignant solid tumors. Oncogene 27, 4385–4391 (2008). · DOI
  4. Pendergast, A. M. The Abl family kinases: mechanisms of regulation and signaling. Adv. Cancer Res. 85, 51–100 (2002). · DOI
  5. Colicelli, J. ABL tyrosine kinases: evolution of function, regulation, and specificity. Sci. Signal. 3, re6 (2010). · DOI
  6. Bradley, W. D. & Koleske, A. J. Regulation of cell migration and morphogenesis by Abl-family kinases: emerging mechanisms and physiological contexts. J. Cell Sci. 122, 3441–3454 (2009). · DOI
  7. Jones, R. B., Gordus, A., Krall, J. A. & MacBeath, G. A quantitative protein interaction network for the ErbB receptors using protein microarrays. Nature 439, 168–174 (2006). · DOI
  8. Srinivasan, D. & Plattner, R. Activation of Abl tyrosine kinases promotes invasion of aggressive breast cancer cells. Cancer Res. 66, 5648–5655 (2006). · DOI
  9. Yang, L., Lin, C. & Liu, Z. R. P68 RNA helicase mediates PDGF-induced epithelial mesenchymal transition by displacing Axin from β-catenin. Cell 127, 139–155 (2006). · DOI
  10. Rikova, K. et al. Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell 131, 1190–1203 (2007). · DOI · Paper page
  11. Lin, J. et al. Oncogenic activation of c-Abl in non-small cell lung cancer cells lacking FUS1 expression: inhibition of c-Abl by the tumor suppressor gene product Fus1. Oncogene 26, 6989–6996 (2007). · DOI
  12. Wu, C. J. et al. A predictive phosphorylation signature of lung cancer. PLoS ONE 4, e7994 (2009). · DOI
  13. Carretero, J. et al. Integrative genomic and proteomic analyses identify targets for Lkb1-deficient metastatic lung tumors. Cancer Cell 17, 547–559 (2010). · DOI
  14. Drake, J. M. et al. Oncogene-specific activation of tyrosine kinase networks during prostate cancer progression. Proc. Natl Acad. Sci. USA 109, 1643–1648 (2012). · DOI
  15. Furlan, A. et al. Abl interconnects oncogenic Met and p53 core pathways in cancer cells. Cell Death Differ. 18, 1608–1616 (2011). · DOI
  16. Ganguly, S. S. et al. c-Abl and Arg are activated in human primary melanomas, promote melanoma cell invasion via distinct pathways, and drive metastatic progression. Oncogene 31, 1804–1816 (2012). References 8 and 16 showed that ABL kinases are required for the invasion of breast cancer cells and melanoma. · DOI
  17. Sos, M. L. et al. Predicting drug susceptibility of non-small cell lung cancers based on genetic lesions. J. Clin. Invest. 119, 1727–1740 (2009). · DOI
  18. Simpson, L. et al. Renal medullary carcinoma and ABL gene amplification. J. Urol. 173, 1883–1888 (2005). · DOI
  19. Behbahani, T. E. et al. Tyrosine kinase expression profile in clear cell renal cell carcinoma. World J. Urol. 30, 559–565 (2012). · DOI
  20. Schwartzberg, P. L. et al. Mice homozygous for the ablm1 mutation show poor viability and depletion of selected B and T cell populations. Cell 65, 1165–1175 (1991). · DOI
  21. Tybulewicz, V. L., Crawford, C. E., Jackson, P. K., Bronson, R. T. & Mulligan, R. C. Neonatal lethality and lymphopenia in mice with a homozygous disruption of the c-abl proto-oncogene. Cell 65, 1153–1163 (1991). References 22 and 23 describe the consequences of genetic inactivation of the murine Abl1 gene, which resulted in immune deficits and decreased viability. · DOI
  22. Qiu, Z., Cang, Y. & Goff, S. P. Abl family tyrosine kinases are essential for basement membrane integrity and cortical lamination in the cerebellum. J. Neurosci. 30, 14430–14439 (2010). · DOI
  23. Li, B. et al. Mice deficient in Abl are osteoporotic and have defects in osteoblast maturation. Nature Genet. 24, 304–308 (2000). · DOI
  24. Kua, H. Y. et al. c-Abl promotes osteoblast expansion by differentially regulating canonical and non-canonical BMP pathways and p16INK4a expression. Nature Cell Biol. 14, 727–737 (2012). · DOI
  25. Koleske, A. J. et al. Essential roles for the Abl and Arg tyrosine kinases in neurulation. Neuron 21, 1259–1272 (1998). This hallmark paper revealed that genetic inactivation of murine Abl1 and Abl2 resulted in embryonic lethality, demonstrating that these two protein kinases have some crucial redundant functions during development. · DOI
  26. Gourley, S. L., Koleske, A. J. & Taylor, J. R. Loss of dendrite stabilization by the Abl-related gene (Arg) kinase regulates behavioral flexibility and sensitivity to cocaine. Proc. Natl Acad. Sci. USA 106, 16859–16864 (2009). · DOI
  27. Van Etten, R. A. et al. The COOH terminus of the c-Abl tyrosine kinase contains distinct F− and G-actin binding domains with bundling activity. J. Cell Biol. 124, 325–340 (1994). · DOI
  28. Wang, Y., Miller, A. L., Mooseker, M. S. & Koleske, A. J. The Abl-related gene (Arg) nonreceptor tyrosine kinase uses two F-actin-binding domains to bundle F-actin. Proc. Natl Acad. Sci. USA 98, 14865–14870 (2001). · DOI
  29. Miller, A. L., Wang, Y., Mooseker, M. S. & Koleske, A. J. The Abl-related gene (Arg) requires its F-actin-microtubule cross-linking activity to regulate lamellipodial dynamics during fibroblast adhesion. J. Cell Biol. 165, 407–419 (2004). · DOI
  30. Zandy, N. L., Playford, M. & Pendergast, A. M. Abl tyrosine kinases regulate cell-cell adhesion through Rho GTPases. Proc. Natl Acad. Sci. USA 104, 17686–17691 (2007). · DOI
  31. Smith-Pearson, P. S., Greuber, E. K., Yogalingam, G. & Pendergast, A. M. Abl kinases are required for invadopodia formation and chemokine-induced invasion. J. Biol. Chem. 285, 40201–40211 (2010). · DOI
  32. Greuber, E. K. & Pendergast, A. M. Abl family kinases regulate FcγR-mediated phagocytosis in murine macrophages. J. Immunol. 189, 5382–5392 (2012). · DOI
  33. Hantschel, O. & Superti-Furga, G. Regulation of the c-Abl and Bcr-Abl tyrosine kinases. Nature Rev. Mol. Cell. Biol. 5, 33–44 (2004). · DOI
  34. Hantschel, O. et al. A myristoyl/phosphotyrosine switch regulates c-Abl. Cell 112, 845–857 (2003). · DOI
  35. Plattner, R. et al. A new link between the c-Abl tyrosine kinase and phosphoinositide signalling through PLC-γ1. Nature Cell Biol. 5, 309–319 (2003). References 36 and 37 showed that regulation of ABL kinases is partly mediated by lipids through distinct mechanisms. Reference 36 showed that the intramolecular interaction of the myristoylated residue in the ABL N terminus with a hydrophobic pocket in the kinase domain stabilizes the auto-inhibited conformation of the kinase. Reference 37 showed that PIP2 inhibits ABL1 activity in vitro and in cells, and that decreasing PIP2 cellular levels by PLCγ1-mediated hydrolysis or dephosphorylation by an inositol-polyphosphate phosphatase results in dramatic increases in ABL kinase activity. · DOI
  36. Cao, X., Tanis, K. Q., Koleske, A. J. & Colicelli, J. Enhancement of ABL kinase catalytic efficiency by a direct binding regulator is independent of other regulatory mechanisms. J. Biol. Chem. 283, 31401–31407 (2008). · DOI
  37. Wen, S. T. & Van Etten, R. A. The PAG gene product, a stress-induced protein with antioxidant properties, is an Abl SH3-binding protein and a physiological inhibitor of c-Abl tyrosine kinase activity. Genes Dev. 11, 2456–2467 (1997). · DOI
  38. Cong, F. et al. Cytoskeletal protein PSTPIP1 directs the PEST-type protein tyrosine phosphatase to the c-Abl kinase to mediate Abl dephosphorylation. Mol. Cell 6, 1413–1423 (2000). · DOI
  39. Tanis, K. Q., Veach, D., Duewel, H. S., Bornmann, W. G. & Koleske, A. J. Two distinct phosphorylation pathways have additive effects on Abl family kinase activation. Mol. Cell. Biol. 23, 3884–3896 (2003). · DOI
  40. Echarri, A. & Pendergast, A. M. Activated c-Abl is degraded by the ubiquitin-dependent proteasome pathway. Curr. Biol. 11, 1759–1765 (2001). · DOI
  41. Wong, S. & Witte, O. N. The BCR-ABL story: bench to bedside and back. Annu. Rev. Immunol. 22, 247–306 (2004). · DOI
  42. Kantarjian, H. M. et al. Significance of the P210 versus P190 molecular abnormalities in adults with Philadelphia chromosome-positive acute leukemia. Blood 78, 2411–2418 (1991). · DOI
  43. Suryanarayan, K. et al. Consistent involvement of the bcr gene by 9;22 breakpoints in pediatric acute leukemias. Blood 77, 324–330 (1991). · DOI
  44. Pane, F. et al. Neutrophilic-chronic myeloid leukemia: a distinct disease with a specific molecular marker (BCR/ABL with C3/A2 junction). Blood 88, 2410–2414 (1996). · DOI
  45. Wilson, G. et al. BCR-ABL transcript with an e19a2 (c3a2) junction in classical chronic myeloid leukemia. Blood 89, 3064 (1997). · DOI
  46. Ren, R. Mechanisms of BCR-ABL in the pathogenesis of chronic myelogenous leukaemia. Nature Rev. Cancer 5, 172–183 (2005). · DOI
  47. O'Hare, T., Zabriskie, M. S., Eiring, A. M. & Deininger, M. W. Pushing the limits of targeted therapy in chronic myeloid leukaemia. Nature Rev. Cancer 12, 513–526 (2012). · DOI
  48. McWhirter, J. R. & Wang, J. Y. Activation of tyrosinase kinase and microfilament-binding functions of c-abl by bcr sequences in bcr/abl fusion proteins. Mol. Cell. Biol. 11, 1553–1565 (1991). · DOI
  49. Muller, A. J. et al. BCR first exon sequences specifically activate the BCR/ABL tyrosine kinase oncogene of Philadelphia chromosome-positive human leukemias. Mol. Cell. Biol. 11, 1785–1792 (1991). · DOI
  50. Reuther, J. Y., Reuther, G. W., Cortez, D., Pendergast, A. M. & Baldwin, A. S. Jr. A requirement for NF-κB activation in Bcr-Abl-mediated transformation. Genes Dev. 12, 968–981 (1998). · DOI
  51. Titz, B. et al. The proximal signaling network of the BCR-ABL1 oncogene shows a modular organization. Oncogene 29, 5895–5910 (2010). · DOI
  52. Gu, J. J. et al. Abl family kinases modulate T cell-mediated inflammation and chemokine-induced migration through the adaptor HEF1 and the GTPase Rap1. Sci. Signal. 5, ra51 (2012). This manuscript established a requirement for both ABL1 and ABL2 in chemokine-induced polarity and migration in T cells. A novel pathway was identified linking ABL kinases to HEF1-mediated regulation of RAP1A during chemokine-induced migration and polarization. · DOI
  53. Zhang, J., Yang, P. L. & Gray, N. S. Targeting cancer with small molecule kinase inhibitors. Nature Rev. Cancer 9, 28–39 (2009). · DOI
  54. Zhang, J. et al. Targeting Bcr-Abl by combining allosteric with ATP-binding-site inhibitors. Nature 463, 501–506 (2010). This paper describes allosteric inhibitors specific for the ABL kinases that target the myristate-binding pocket and impair downstream signalling, as well as BCR–ABL-induced leukaemia in mice. · DOI
  55. Hagemeijer, A. & Graux, C. ABL1 rearrangements in T-cell acute lymphoblastic leukemia. Genes Chromosomes Cancer 49, 299–308 (2010). · DOI
  56. De Braekeleer, E. et al. ABL1 fusion genes in hematological malignancies: a review. Eur. J. Haematol. 86, 361–371 (2011). · DOI
  57. Ernst, T. et al. Identification of FOXP1 and SNX2 as novel ABL1 fusion partners in acute lymphoblastic leukaemia. Br. J. Haematol. 153, 43–46 (2011). · DOI
  58. De Braekeleer, E. et al. ETV6 fusion genes in hematological malignancies: a review. Leuk. Res. 36, 945–961 (2012). · DOI
  59. De Keersmaecker, K. et al. Kinase activation and transformation by NUP214-ABL1 is dependent on the context of the nuclear pore. Mol. Cell 31, 134–142 (2008). · DOI
  60. Koos, B. et al. The tyrosine kinase c-Abl promotes proliferation and is expressed in atypical teratoid and malignant rhabdoid tumors. Cancer 116, 5075–5081 (2010). · DOI
  61. Chen, G. et al. Radiation-induced assembly of Rad51 and Rad52 recombination complex requires ATM and c-Abl. J. Biol. Chem. 274, 12748–12752 (1999). · DOI · Paper page
  62. Crnogorac-Jurcevic, T. et al. Expression profiling of microdissected pancreatic adenocarcinomas. Oncogene 21, 4587–4594 (2002). · DOI
  63. Wu, C. W. et al. Arg tyrosine kinase expression in human gastric adenocarcinoma is associated with vessel invasion. Anticancer Res. 23, 205–210 (2003).
  64. Greenman, C. et al. Patterns of somatic mutation in human cancer genomes. Nature 446, 153–158 (2007). · DOI
  65. Ruhe, J. E. et al. Genetic alterations in the tyrosine kinase transcriptome of human cancer cell lines. Cancer Res. 67, 11368–11376 (2007). · DOI
  66. Plattner, R., Kadlec, L., DeMali, K. A., Kazlauskas, A. & Pendergast, A. M. c-Abl is activated by growth factors and Src family kinases and has a role in the cellular response to PDGF. Genes Dev. 13, 2400–2411 (1999). This manuscript demonstrated for the first time that endogenous ABL1 (cellular ABL) is activated by growth factors PDGF and EGF, and also by activated SRC family kinases. · DOI
  67. Sirvent, A., Boureux, A., Simon, V., Leroy, C. & Roche, S. The tyrosine kinase Abl is required for Src-transforming activity in mouse fibroblasts and human breast cancer cells. Oncogene 26, 7313–7323 (2007). · DOI
  68. Srinivasan, D., Sims, J. T. & Plattner, R. Aggressive breast cancer cells are dependent on activated Abl kinases for proliferation, anchorage-independent growth and survival. Oncogene 27, 1095–1105 (2008). This manuscript showed that, similar to growth factor-stimulated fibroblasts, maximal proliferation and survival of some breast cancer cells required the activity of ABL kinases. · DOI
  69. Mader, C. C. et al. An EGFR-Src-Arg-cortactin pathway mediates functional maturation of invadopodia and breast cancer cell invasion. Cancer Res. 71, 1730–1741 (2011). References 33 and 73 showed a role for ABL kinases in the formation and function of invadopodia. ABL2 localizes to invadopodia and regulates the function of invadopodia components including cortactin and MT1-MMP in breast cancer cells. · DOI
  70. Iavarone, C. et al. Activation of the Erk8 mitogen-activated protein (MAP) kinase by RET/PTC3, a constitutively active form of the RET proto-oncogene. J. Biol. Chem. 281, 10567–10576 (2006). · DOI
  71. Hantschel, O., Rix, U. & Superti-Furga, G. Target spectrum of the BCR-ABL inhibitors imatinib, nilotinib and dasatinib. Leuk. Lymphoma 49, 615–619 (2008). · DOI · Paper page
  72. Packer, L. M. et al. Nilotinib and MEK inhibitors induce synthetic lethality through paradoxical activation of RAF in drug-resistant chronic myeloid leukemia. Cancer Cell 20, 715–727 (2011). · DOI
  73. Yuan, B. Z., Jefferson, A. M., Popescu, N. C. & Reynolds, S. H. Aberrant gene expression in human non small cell lung carcinoma cells exposed to demethylating agent 5-aza-2′-deoxycytidine. Neoplasia 6, 412–419 (2004). · DOI
  74. Sirvent, A., Benistant, C. & Roche, S. Cytoplasmic signalling by the c-Abl tyrosine kinase in normal and cancer cells. Biol. Cell 100, 617–631 (2008). · DOI
  75. Anastas, J. N. & Moon, R. T. WNT signalling pathways as therapeutic targets in cancer. Nature Rev. Cancer 13, 11–26 (2013). · DOI
  76. Ikushima, H. & Miyazono, K. TGFβ signalling: a complex web in cancer progression. Nature Rev. Cancer 10, 415–424 (2010). · DOI
  77. Harvey, K. F., Zhang, X. & Thomas, D. M. The Hippo pathway and human cancer. Nature Rev. Cancer 13, 246–257 (2013). · DOI
  78. Noren, N. K., Foos, G., Hauser, C. A. & Pasquale, E. B. The EphB4 receptor suppresses breast cancer cell tumorigenicity through an Abl-Crk pathway. Nature Cell Biol. 8, 815–825 (2006). · DOI
  79. Allington, T. M., Galliher-Beckley, A. J. & Schiemann, W. P. Activated Abl kinase inhibits oncogenic transforming growth factor-β signaling and tumorigenesis in mammary tumors. FASEB J. 23, 4231–4243 (2009). · DOI
  80. Gil-Henn, H. et al. Arg/Abl2 promotes invasion and attenuates proliferation of breast cancer in vivo. Oncogene 31, 1804–1816 (2012). · DOI
  81. Li, X. et al. c-Abl and Arg tyrosine kinases regulate lysosomal degradation of the oncoprotein Galectin-3. Cell Death Differ. 17, 1277–1287 (2010). · DOI
  82. Shaul, Y. & Ben-Yehoyada, M. Role of c-Abl in the DNA damage stress response. Cell Res. 15, 33–35 (2005). · DOI
  83. Sun, X. et al. Activation of the cytoplasmic c-Abl tyrosine kinase by reactive oxygen species. J. Biol. Chem. 275, 17237–17240 (2000). · DOI
  84. Cao, C. et al. The ARG tyrosine kinase interacts with Siva-1 in the apoptotic response to oxidative stress. J. Biol. Chem. 276, 11465–11468 (2001). · DOI
  85. Hopkins, S. et al. Mig6 is a sensor of EGF receptor inactivation that directly activates c-Abl to induce apoptosis during epithelial homeostasis. Dev. Cell 23, 547–559 (2012). · DOI
  86. Grek, C. L. & Tew, K. D. Redox metabolism and malignancy. Curr. Opin. Pharmacol. 10, 362–368 (2010). · DOI
  87. Finkel, T. & Holbrook, N. J. Oxidants, oxidative stress and the biology of ageing. Nature 408, 239–247 (2000). · DOI · Paper page
  88. Klaunig, J. E. & Kamendulis, L. M. The role of oxidative stress in carcinogenesis. Annu. Rev. Pharmacol. Toxicol. 44, 239–267 (2004). · DOI
  89. Hileman, E. O., Liu, J., Albitar, M., Keating, M. J. & Huang, P. Intrinsic oxidative stress in cancer cells: a biochemical basis for therapeutic selectivity. Cancer Chemother. Pharmacol. 53, 209–219 (2004). · DOI
  90. Cao, C. et al. Ubiquitination and degradation of the Arg tyrosine kinase is regulated by oxidative stress. Oncogene 24, 2433–2440 (2005). · DOI
  91. Cao, C., Leng, Y., Li, C. & Kufe, D. Functional interaction between the c-Abl and Arg protein-tyrosine kinases in the oxidative stress response. J. Biol. Chem. 278, 12961–12967 (2003). · DOI
  92. Kharbanda, S. et al. Activation of the c-Abl tyrosine kinase in the stress response to DNA-damaging agents. Nature 376, 785–788 (1995). · DOI
  93. Yuan, Z. M. et al. Role for c-Abl tyrosine kinase in growth arrest response to DNA damage. Nature 382, 272–274 (1996). · DOI
  94. Whang, Y. E. et al. c-Abl is required for development and optimal cell proliferation in the context of p53 deficiency. Proc. Natl Acad. Sci. USA 97, 5486–5491 (2000). · DOI
  95. Furstoss, O. et al. c-Abl is an effector of Src for growth factor-induced c-myc expression and DNA synthesis. EMBO J. 21, 514–524 (2002). · DOI
  96. Goldberg, Z. et al. Tyrosine phosphorylation of Mdm2 by c-Abl: implications for p53 regulation. EMBO J. 21, 3715–3727 (2002). · DOI
  97. Agami, R., Blandino, G., Oren, M. & Shaul, Y. Interaction of c-Abl and p73α and their collaboration to induce apoptosis. Nature 399, 809–813 (1999). · DOI
  98. Yuan, Z. M. et al. p73 is regulated by tyrosine kinase c-Abl in the apoptotic response to DNA damage. Nature 399, 814–817 (1999). · DOI
  99. Levav-Cohen, Y. et al. C-Abl as a modulator of p53. Biochem. Biophys. Res. Commun. 331, 737–749 (2005). · DOI
  100. Feigin, M. E. & Muthuswamy, S. K. Polarity proteins regulate mammalian cell-cell junctions and cancer pathogenesis. Curr. Opin. Cell Biol. 21, 694–700 (2009). · DOI
  101. Baum, B. & Perrimon, N. Spatial control of the actin cytoskeleton in Drosophila epithelial cells. Nature Cell Biol. 3, 883–890 (2001). · DOI
  102. Grevengoed, E. E., Loureiro, J. J., Jesse, T. L. & Peifer, M. Abelson kinase regulates epithelial morphogenesis in Drosophila. J. Cell Biol. 155, 1185–1198 (2001). · DOI
  103. Fox, D. T. & Peifer, M. Abelson kinase (Abl) and RhoGEF2 regulate actin organization during cell constriction in Drosophila. Development 134, 567–578 (2007). · DOI
  104. Tamada, M., Farrell, D. L. & Zallen, J. A. Abl regulates planar polarized junctional dynamics through β-catenin tyrosine phosphorylation. Dev. Cell 22, 309–319 (2012). · DOI
  105. Singh, J., Aaronson, S. A. & Mlodzik, M. Drosophila Abelson kinase mediates cell invasion and proliferation through two distinct MAPK pathways. Oncogene 29, 4033–4045 (2010). · DOI
  106. Li, R. & Pendergast, A. M. Arg kinase regulates epithelial cell polarity by targeting β1-integrin and small GTPase pathways. Curr. Biol. 21, 1534–1542 (2011). This work describes a role for activated ABL kinases in the regulation of epithelial apical–basal polarity. Expression of active ABL2 induces striking inversion of epithelial apical–basal polarity by disrupting β1 integrin signalling and laminin assembly. Thus, activated ABL kinases may be involved in early steps of tumour initiation. · DOI
  107. Gonzalez, C. Spindle orientation, asymmetric division and tumour suppression in Drosophila stem cells. Nature Rev. Genet. 8, 462–472 (2007). · DOI
  108. Fleming, E. S., Temchin, M., Wu, Q., Maggio-Price, L. & Tirnauer, J. S. Spindle misorientation in tumors from APCmin/+ mice. Mol. Carcinog. 48, 592–598 (2009). · DOI
  109. Knoblich, J. A. Mechanisms of asymmetric stem cell division. Cell 132, 583–597 (2008). · DOI
  110. Matsumura, S. et al. ABL1 regulates spindle orientation in adherent cells and mammalian skin. Nature Commun. 3, 626 (2012). · DOI
  111. Yang, J. & Weinberg, R. A. Epithelial-mesenchymal transition: at the crossroads of development and tumor metastasis. Dev. Cell 14, 818–829 (2008). · DOI
  112. Yasmeen, A., Alachkar, A., Dekhil, H., Gambacorti-Passerini, C. & Al Moustafa, A. E. Locking Src/Abl tyrosine kinase activities regulate cell differentiation and invasion of human cervical cancer cells expressing, E6/E7 oncoproteins of high-risk, HPV. J. Oncol. 530130 (2010). · DOI
  113. Suh, Y. et al. Claudin-1 induces epithelial-mesenchymal transition through activation of the c-Abl-ERK signaling pathway in human liver cells. Oncogene 19 Nov 2012 (doi:10.1038/onc.2012.505). · DOI
  114. Shapiro, I. M. et al. An EMT-driven alternative splicing program occurs in human breast cancer and modulates cellular phenotype. PLoS Genet. 7, e1002218 (2011). · DOI
  115. Weigel, M. T. et al. Enhanced expression of the PDGFR/Abl signaling pathway in aromatase inhibitor-resistant breast cancer. Ann. Oncol. 24, 126–133 (2012). · DOI
  116. Yoon, C. H. et al. Claudin-1 acts through c-Abl-protein kinase Cδ (PKCδ) signaling and has a causal role in the acquisition of invasive capacity in human liver cells. J. Biol. Chem. 285, 226–233 (2010). · DOI
  117. Sun, X. et al. Abl interactor 1 regulates Src-Id1-matrix metalloproteinase 9 axis and is required for invadopodia formation, extracellular matrix degradation and tumor growth of human breast cancer cells. Carcinogenesis 30, 2109–2116 (2009). · DOI
  118. Burton, E. A., Oliver, T. N. & Pendergast, A. M. Abl kinases regulate actin comet tail elongation via an N-WASP-dependent pathway. Mol. Cell. Biol. 25, 8834–8843 (2005). · DOI
  119. Oser, M. et al. Cortactin regulates cofilin and N-WASp activities to control the stages of invadopodium assembly and maturation. J. Cell Biol. 186, 571–587 (2009). · DOI
  120. Oser, M. et al. Specific tyrosine phosphorylation sites on cortactin regulate Nck1-dependent actin polymerization in invadopodia. J. Cell Sci. 123, 3662–3673 (2010). · DOI
  121. Singh, M., Cowell, L., Seo, S., O'Neill, G. & Golemis, E. Molecular basis for HEF1/NEDD9/Cas-L action as a multifunctional co-ordinator of invasion, apoptosis and cell cycle. Cell Biochem. Biophys. 48, 54–72 (2007). · DOI
  122. Hantschel, O., Grebien, F. & Superti-Furga, G. The growing arsenal of ATP-competitive and allosteric inhibitors of BCR-ABL. Cancer Res. 72, 4890–4895 (2012). · DOI
  123. Roychowdhury, S. & Talpaz, M. Managing resistance in chronic myeloid leukemia. Blood Rev. 25, 279–290 (2011). · DOI
  124. Grebien, F. et al. Targeting the SH2-kinase interface in Bcr-Abl inhibits leukemogenesis. Cell 147, 306–319 (2011). · DOI
  125. Ganguly, S. S. & Plattner, R. Activation of abl family kinases in solid tumors. Genes Cancer 3, 414–425 (2012). · DOI
  126. Puls, L. N., Eadens, M. & Messersmith, W. Current status of SRC inhibitors in solid tumor malignancies. Oncologist 16, 566–578 (2011). · DOI · Paper page
  127. Lee, M. J. et al. Sequential application of anticancer drugs enhances cell death by rewiring apoptotic signaling networks. Cell 149, 780–794 (2012). · DOI
  128. Duncan, J. S. et al. Dynamic reprogramming of the kinome in response to targeted MEK inhibition in triple-negative breast cancer. Cell 149, 307–321 (2012). References 136 and 137 are two excellent papers that demonstrate the dynamic reprogramming of cancer cells in response to kinase inhibitors and show that understanding these responses will permit the rational design of combination therapies to overcome resistance to chemotherapy. · DOI · Paper page
  129. Su, F. et al. RAS mutations in cutaneous squamous-cell carcinomas in patients treated with BRAF inhibitors. N. Engl. J. Med. 366, 207–215 (2012). · DOI
  130. Weigel, M. T. et al. Preclinical and clinical studies of estrogen deprivation support the PDGF/Abl pathway as a novel therapeutic target for overcoming endocrine resistance in breast cancer. Breast Cancer Res. 14, R78 (2012). · DOI
  131. He, X. et al. c-Abl regulates estrogen receptor α transcription activity through its stabilization by phosphorylation. Oncogene 29, 2238–2251 (2010). · DOI
  132. Zhao, H. et al. Enhanced resistance to tamoxifen by the c-ABL proto-oncogene in breast cancer. Neoplasia 12, 214–223 (2010). · DOI
  133. Sims, J. T. et al. STI571 sensitizes breast cancer cells to 5-fluorouracil, cisplatin and camptothecin in a cell type-specific manner. Biochem. Pharmacol. 78, 249–260 (2009). · DOI
  134. Weigel, M. T. et al. Combination of imatinib and vinorelbine enhances cell growth inhibition in breast cancer cells via PDGFR β signalling. Cancer Lett. 273, 70–79 (2009). · DOI
  135. Lo, Y. H., Ho, P. C., Zhao, H. & Wang, S. C. Inhibition of c-ABL sensitizes breast cancer cells to the dual ErbB receptor tyrosine kinase inhibitor lapatinib Anticancer Res. 31, 789–795 (2011).
  136. Wetzel, D. M., McMahon-Pratt, D. & Koleske, A. J. The Abl and Arg kinases mediate distinct modes of phagocytosis and are required for maximal Leishmania infection. Mol. Cell. Biol. 32, 3176–3186 (2012). · DOI
  137. Gu, J. J., Zhang, N., He, Y. W., Koleske, A. J. & Pendergast, A. M. Defective T cell development and function in the absence of Abelson kinases. J. Immunol. 179, 7334–7343 (2007). · DOI
  138. Orimo, A. & Weinberg, R. A. Stromal fibroblasts in cancer: a novel tumor-promoting cell type. Cell Cycle 5, 1597–1601 (2006). · DOI
  139. DeNardo, D. G., Andreu, P. & Coussens, L. M. Interactions between lymphocytes and myeloid cells regulate pro- versus anti-tumor immunity. Cancer Metastasis Rev. 29, 309–316 (2010). · DOI
  140. Millot, F. et al. Imatinib is effective in children with previously untreated chronic myelogenous leukemia in early chronic phase: results of the French national phase IV trial. J. Clin. Oncol. 29, 2827–2832 (2011). · DOI
  141. Schultz, K. R. et al. Improved early event-free survival with imatinib in Philadelphia chromosome-positive acute lymphoblastic leukemia: a children's oncology group study. J. Clin. Oncol. 27, 5175–5181 (2009). · DOI
  142. O'Hare, T. et al. AP24534, a pan-BCR-ABL inhibitor for chronic myeloid leukemia, potently inhibits the T315I mutant and overcomes mutation-based resistance. Cancer Cell 16, 401–412 (2009). · DOI
  143. Bianchi, C. et al. Eight full-length abelson related gene (Arg) isoforms are constitutively expressed in caki-1 cell line and cell distribution of two isoforms has been analyzed after transfection. J. Cell Biochem. 105, 1219–1227 (2008). · DOI
  144. Adrian, F. J. et al. Allosteric inhibitors of Bcr-abl-dependent cell proliferation. Nature Chem. Biol. 2, 95–102 (2006). · DOI
  145. Choi, Y. et al. N-myristoylated c-Abl tyrosine kinase localizes to the endoplasmic reticulum upon binding to an allosteric inhibitor. J. Biol. Chem. 284, 29005–29014 (2009). · DOI
  146. Abelson, H. T. & Rabstein, L. S. Lymphosarcoma: virus-induced thymic-independent disease in mice. Cancer Res. 30, 2213–2222 (1970).
  147. Green, P. L., Kaehler, D. A., Bennett, L. M. & Risser, R. Multiple steps are required for the induction of tumors by Abelson murine leukemia virus. J. Virol. 63, 1989–1994 (1989). · DOI

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Metadata

Authors
Greuber, E. K., Smith-Pearson, P., Wang, J., & Pendergast, A. M.
Venue
Nature Reviews Cancer
Published
2013-07-11
Volume
13
Issue
8
Pages
559-571
ISSN
  • 1474-175X
  • 1474-1768
Cited by
432
References
10
Language
en

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