PML inhibits HIF-1α translation and neoangiogenesis through repression of mTOR (original) (raw)

• Hanahan, D. & Folkman, J. Patterns and emerging mechanisms of the angiogenic switch during tumorigenesis. Cell 86, 353–364 (1996)
  Article CAS Google Scholar
• Ferrara, N. Vascular endothelial growth factor: basic science and clinical progress. Endocr. Rev. 25, 581–611 (2004)
  Article CAS Google Scholar
• Semenza, G. L. HIF-1 and tumor progression: pathophysiology and therapeutics. Trends Mol. Med. 8, S62–S67 (2002)
  Article CAS Google Scholar
• de The, H. et al. The PML-RARα fusion mRNA generated by the t(15;17) translocation in acute promyelocytic leukemia encodes a functionally altered RAR. Cell 66, 675–684 (1991)
  Article CAS Google Scholar
• Goddard, A. D., Borrow, J., Freemont, P. S. & Solomon, E. Characterization of a zinc finger gene disrupted by the t(15;17) in acute promyelocytic leukemia. Science 254, 1371–1374 (1991)
  Article ADS CAS Google Scholar
• Kakizuka, A. et al. Chromosomal translocation t(15;17) in human acute promyelocytic leukemia fuses RARα with a novel putative transcription factor, PML. Cell 66, 663–674 (1991)
  Article CAS Google Scholar
• Pandolfi, P. P. et al. Structure and origin of the acute promyelocytic leukemia myl/RARα cDNA and characterization of its retinoid-binding and transactivation properties. Oncogene 6, 1285–1292 (1991)
  CAS PubMed Google Scholar
• Rego, E. M. et al. Role of promyelocytic leukemia (PML) protein in tumor suppression. J. Exp. Med. 193, 521–529 (2001)
  Article CAS Google Scholar
• Salomoni, P. & Pandolfi, P. P. The role of PML in tumor suppression. Cell 108, 165–170 (2002)
  Article CAS Google Scholar
• Wang, Z. G. et al. PML is essential for multiple apoptotic pathways. Nature Genet. 20, 266–272 (1998)
  Article CAS Google Scholar
• Wang, Z. G. et al. Role of PML in cell growth and the retinoic acid pathway. Science 279, 1547–1551 (1998)
  Article ADS CAS Google Scholar
• Trotman, L. C. et al. Identification of a tumour suppressor network opposing nuclear Akt function. Nature 441, 523–527 (2006)
  Article ADS CAS Google Scholar
• Koken, M. H. et al. The PML growth-suppressor has an altered expression in human oncogenesis. Oncogene 10, 1315–1324 (1995)
  CAS PubMed Google Scholar
• Gambacorta, M. et al. Heterogeneous nuclear expression of the promyelocytic leukemia (PML) protein in normal and neoplastic human tissues. Am. J. Pathol. 149, 2023–2035 (1996)
  CAS PubMed PubMed Central Google Scholar
• Zhang, P. et al. Lack of expression for the suppressor PML in human small cell lung carcinoma. Int. J. Cancer 85, 599–605 (2000)
  Article CAS Google Scholar
• Gurrieri, C. et al. Loss of the tumor suppressor PML in human cancers of multiple histologic origins. J. Natl Cancer Inst. 96, 269–279 (2004)
  Article CAS Google Scholar
• Lin, H. K., Bergmann, S. & Pandolfi, P. P. Cytoplasmic PML function in TGF-β signalling. Nature 431, 205–211 (2004)
  Article ADS CAS Google Scholar
• Takahashi, Y., Lallemand-Breitenbach, V., Zhu, J. & de The, H. PML nuclear bodies and apoptosis. Oncogene 23, 2819–2824 (2004)
  Article CAS Google Scholar
• Marti, H. H. & Risau, W. Angiogenesis in ischemic disease. Thromb. Haemost. 82 (suppl. 1), 44–52 (1999)
  PubMed Google Scholar
• Rafii, S. & Lyden, D. Therapeutic stem and progenitor cell transplantation for organ vascularization and regeneration. Nature Med. 9, 702–712 (2003)
  Article CAS Google Scholar
• Rabbany, S. Y., Heissig, B., Hattori, K. & Rafii, S. Molecular pathways regulating mobilization of marrow-derived stem cells for tissue revascularization. Trends Mol. Med. 9, 109–117 (2003)
  Article CAS Google Scholar
• Lyden, D. et al. Impaired recruitment of bone-marrow-derived endothelial and hematopoietic precursor cells blocks tumor angiogenesis and growth. Nature Med. 7, 1194–1201 (2001)
  Article CAS Google Scholar
• Amano, K. et al. Mechanism for IL-1β-mediated neovascularization unmasked by IL-1β knock-out mice. J. Mol. Cell. Cardiol. 36, 469–480 (2004)
  Article CAS Google Scholar
• Semenza, G. L. Targeting HIF-1 for cancer therapy. Nature Rev. Cancer 3, 721–732 (2003)
  Article CAS Google Scholar
• Kaelin, W. G. Jr. How oxygen makes its presence felt. Genes Dev. 16, 1441–1445 (2002)
  Article CAS Google Scholar
• Brahimi-Horn, C. & Pouyssegur, J. When hypoxia signalling meets the ubiquitin-proteasomal pathway, new targets for cancer therapy. Crit. Rev. Oncol. Hematol. 53, 115–123 (2005)
  Article Google Scholar
• Arsham, A. M., Howell, J. J. & Simon, M. C. A novel hypoxia-inducible factor-independent hypoxic response regulating mammalian target of rapamycin and its targets. J. Biol. Chem. 278, 29655–29660 (2003)
  Article CAS Google Scholar
• Brugarolas, J. et al. Regulation of mTOR function in response to hypoxia by REDD1 and the TSC1/TSC2 tumor suppressor complex. Genes Dev. 18, 2893–2904 (2004)
  Article CAS Google Scholar
• Liu, L. et al. Hypoxia-induced energy stress regulates mRNA translation and cell growth. Mol. Cell 21, 521–531 (2006)
  Article Google Scholar
• Dufner, A. & Thomas, G. Ribosomal S6 kinase signaling and the control of translation. Exp. Cell Res. 253, 100–109 (1999)
  Article CAS Google Scholar
• Harrington, L. S., Findlay, G. M. & Lamb, R. F. Restraining PI3K: mTOR signalling goes back to the membrane. Trends Biochem. Sci. 30, 35–42 (2005)
  Article CAS Google Scholar
• Martin, D. E. & Hall, M. N. The expanding TOR signaling network. Curr. Opin. Cell Biol. 17, 158–166 (2005)
  Article CAS Google Scholar
• Long, X., Ortiz-Vega, S. & Avruch, J. Rheb binding to mammalian target of rapamycin (mTOR) is regulated by amino acid sufficiency. J. Biol. Chem. 280, 23433–23436 (2005)
  Article CAS Google Scholar
• Kim, J. E. & Chen, J. Cytoplasmic-nuclear shuttling of FKBP12-rapamycin-associated protein is involved in rapamycin-sensitive signaling and translation initiation. Proc. Natl Acad. Sci. USA 97, 14340–14345 (2000)
  Article ADS CAS Google Scholar
• Park, I. H., Bachmann, R., Shirazi, H. & Chen, J. Regulation of ribosomal S6 kinase 2 by mammalian target of rapamycin. J. Biol. Chem. 277, 31423–31429 (2002)
  Article CAS Google Scholar
• Paglin, S. et al. Rapamycin-sensitive pathway regulates mitochondrial membrane potential, autophagy, and survival in irradiated MCF-7 cells. Cancer Res. 65, 11061–11070 (2005)
  Article CAS Google Scholar
• Jensen, K., Shiels, C. & Freemont, P. S. PML protein isoforms and the RBCC/TRIM motif. Oncogene 20, 7223–7233 (2001)
  Article CAS Google Scholar
• Corada, M. et al. A monoclonal antibody to vascular endothelial-cadherin inhibits tumor angiogenesis without side effects on endothelial permeability. Blood 100, 905–911 (2002)
  Article CAS Google Scholar
• Liao, F. et al. Selective targeting of angiogenic tumor vasculature by vascular endothelial-cadherin antibody inhibits tumor growth without affecting vascular permeability. Cancer Res. 62, 2567–2575 (2002)
  CAS PubMed Google Scholar
• Zhu, J., Lallemand-Breitenbach, V. & de The, H. Pathways of retinoic acid- or arsenic trioxide-induced PML/RARα catabolism, role of oncogene degradation in disease remission. Oncogene 20, 7257–7265 (2001)
  Article CAS Google Scholar
• Lavau, C. et al. The acute promyelocytic leukaemia-associated PML gene is induced by interferon. Oncogene 11, 871–876 (1995)
  CAS PubMed Google Scholar
• Chelbi-Alix, M. K. et al. Induction of the PML protein by interferons in normal and APL cells. Leukemia 9, 2027–2033 (1995)
  CAS PubMed Google Scholar
• Sawyers, C. L. Will mTOR inhibitors make it as cancer drugs? Cancer Cell 4, 343–348 (2003)
  Article CAS Google Scholar
• Vignot, S., Faivre, S., Aguirre, D. & Raymond, E. mTOR-targeted therapy of cancer with rapamycin derivatives. Ann. Oncol. 16, 525–537 (2005)
  Article CAS Google Scholar
• Bernardi, R. et al. PML regulates p53 stability by sequestering Mdm2 to the nucleolus. Nature Cell Biol. 6, 665–672 (2004)
  Article CAS Google Scholar
• Sarbassov, D. D. et al. Rictor, a novel binding partner of mTOR, defines a rapamycin-insensitive and raptor-independent pathway that regulates the cytoskeleton. Curr. Biol. 14, 1296–1302 (2004)
  Article CAS Google Scholar
• Grisendi, S. et al. Role of nucleophosmin in embryonic development and tumorigenesis. Nature 437, 147–153 (2005)
  Article ADS CAS Google Scholar