Stabilization and Enhancement of the Antiapoptotic Activity of Mcl-1 by TCTP

REFERENCES

• Akgul, C., D. A. Moulding, and S. W. Edwards. 2001. Molecular control of neutrophil apoptosis. FEBS Lett. 487:318–322.
   PubMed Web of Science ®Google Scholar
• Altmeyer, A., R. C. Simmons, S. Krajewski, J. C. Reed, G. W. Bornkamm, and S. Chen-Kiang. 1997. Reversal of EBV immortalization precedes apoptosis in IL-6-induced human B-cell terminal differentiation. Immunity 5:667–677.
   Google Scholar
• Bohm, H., R. Benndorf, M. Gaestel, B. Gross, P. Nurnberg, R. Kraft, A. Otto, and H. Bielka. 1989. The growth-related protein P23 of the Ehrlich ascites tumor: translational control, cloning and primary structure. Biochem. Int. 19:277–286.
   PubMedGoogle Scholar
• Brummelkamp, T. R., R. Bernards, and R. Agami. 2002. A system for stable expression of short interfering RNAs in mammalian cells. Science 296:550–553.
   PubMed Web of Science ®Google Scholar
• Cans, C., B. J. Passer, V. Shalak, V. Nancy-Portebois, V. Crible, N. Amzallag, D. Allanic, R. Tufino, M. Argentini, D. Moras, G. Fiucci, B. Goud, M. Mirande, R. Amson, and A. Telerman. 2003. Translationally controlled tumor protein acts as a guanine nucleotide dissociation inhibitor on the translation elongation factor eEF1A. Proc. Natl. Acad. Sci. USA 100:13892–13897.
   PubMed Web of Science ®Google Scholar
• Chao, J. R., J. M. Wang, S. F. Lee, H. W. Peng, Y. H. Lin, C. H. Chou, J. C. Li, H. M. Huang, C. K. Chou, M. L. Kuo, J. J. Yen, and H. F. Yang-Yen. 1998. mcl-1 is an immediate-early gene activated by the granulocyte-macrophage colony-stimulating factor (GM-CSF) signaling pathway and is one component of the GM-CSF viability response. Mol. Cell. Biol. 18:4883–4898.
   PubMed Web of Science ®Google Scholar
• Craig, R. W. 2002. MCL1 provides a window on the role of the BCL2 family in cell proliferation, differentiation, and tumorigenesis. Leukemia 16:444–454.
   PubMed Web of Science ®Google Scholar
• Cuconati, A., C. Mukherjee, D. Perez, and E. White. 2003. DNA damage response and MCL-1 destruction initiate apoptosis in adenovirus-infected cells. Genes Dev. 17:2922–2932.
   PubMed Web of Science ®Google Scholar
• Gachet, Y., S. Tournier, M. Lee, A. Lazaris-Karatzas, T. Poulton, and U. A. Bommer. 1999. The growth-related, translationally controlled protein P23 has properties of a tubulin binding protein and associates transiently with microtubules during the cell cycle. J. Cell Sci. 8:1257–1271.
   Google Scholar
• Heffernan, M., and J. W. Dennis. 1991. Polyoma and hamster papovavirus large T antigen-mediated replication of expression shuttle vectors in Chinese hamster ovary cells. Nucleic Acids Res. 19:85–92.
   PubMed Web of Science ®Google Scholar
• Hsu, S. Y., A. Kaipia, E. McGee, M. Lomeli, and Hsueh, A. J. 1997. Bok is a proapoptotic Bcl-2 protein with restricted expression in reproductive tissues and heterodimerizes with selective antiapoptotic Bcl-2 family members. Proc. Natl. Acad. Sci. USA 94:12401–12406.
   PubMed Web of Science ®Google Scholar
• Huang, H. M., C. J. Huang, and J. J. Yen. 2000. Mcl-1 is a common target of stem cell factor and interleukin-5 for apoptosis prevention activity via MEK/MAPK and PI-3K/Akt pathways. Blood 96:1764–1771.
   PubMed Web of Science ®Google Scholar
• Jourdan, M., J. De Vos, N. Mechti, and B. Klein. 2000. Regulation of Bcl-2-family proteins in myeloma cells by three myeloma survival factors: interleukin-6, interferon-alpha and insulin-like growth factor 1. Cell Death Differ. 7:1244–1252.
   PubMed Web of Science ®Google Scholar
• Karsan, A., E. Yee, K. Kaushansky, and J. M. Harlan. 1996. Cloning of human Bcl-2 homologue: inflammatory cytokines induce human A1 in cultured endothelial cells. Blood 87:3089–3096.
   PubMed Web of Science ®Google Scholar
• Kozopas, K. M., T. Yang, H. L. Buchan, P. Zhou, and R. W. Craig. 1993. Mcl-1, a gene expressed in programmed myeloid cell differentiation has sequence similarity to Bcl2. Proc. Natl. Acad. Sci. USA 90:3516–3520.
   PubMed Web of Science ®Google Scholar
• Leu, C. M., C. Chang, and C. Hu. 2000. Epidermal growth factor (EGF) suppresses staurosporine-induced apoptosis by inducing mcl-1 via the mitogen-activated protein kinase pathway. Oncogene 19:1665–1675.
   PubMedGoogle Scholar
• Li, F., D. Zhang, and K. Fujise. 2001. Characterization of fortilin, a novel antiapoptotic protein. J. Biol. Chem. 276:47542–47549.
   PubMed Web of Science ®Google Scholar
• Lin, E. Y., A. Orlofsky, M. S. Berger, and M. B. Prystowsky. 1993. Characterization of A1, a novel hemopoietic-specific early-response gene with sequence similarity to bcl-2. J. Immunol. 151:1979–1988.
   PubMed Web of Science ®Google Scholar
• Lin, Y. H., C. J. Huang, J. R. Chao, S. T. Chen, S. F. Lee, J. J. Y. Yen, and H. F. Yang-Yen. 2000. Coupling of osteopontin and its cell surface receptor CD44 to the cell survival response elicited by IL-3 or GM-CSF. Mol. Cell. Biol. 20:2734–2742.
   PubMedGoogle Scholar
• Liu, H., H. Perlman, L. J. Pagliari, and R. M. Pope. 2001. Constitutively activated Akt-1 is vital for the survival of human monocyte-differentiated macrophages. Role of Mcl-1, independent of nuclear factor (NF)-κB, Bad, or caspase activatio. J. Exp. Med. 194:113–126.
   PubMed Web of Science ®Google Scholar
• Lomo, J., E. B. Smeland, S. Krajewski, J. C. Reed, and H. K. Blomhoff. 1996. Expression of the Bcl-2 homologue Mcl-1 correlates with survival of peripheral blood B lymphocytes. Cancer Res. 56:40–43.
   PubMed Web of Science ®Google Scholar
• MacDonald, S. M., T. Rafnar, J. Langdon, and L. M. Lichtenstein. 1995. Molecular identification of an IgE-dependent histamine-releasing factor. Science 269:688–690.
   PubMed Web of Science ®Google Scholar
• Moulding, D. A., C. Akgul, M. Derouet, M. R. White, and S. W. Edwards. 2001. BCL-2 family expression in human neutrophils during delayed and accelerated apoptosis. J. Leukoc. Biol. 70:783–792.
   PubMed Web of Science ®Google Scholar
• Moulding, D. A., J. A. Quayle, C. A. Hart, and S. W. Edwards. 1998. Mcl-1 expression in human neutrophils: regulation by cytokines and correlation with cell survival. Blood 92:2495–2502.
   PubMedGoogle Scholar
• Muchmore, S. W., M. Sattler, H. Liang, R. P. Meadows, J. E. Harlan, H. S. Yoon, D. Nettesheim, B. S. Chang, C. B. Thompson, S. L. Wong, S. L. Ng, and S. W. Fesik. 1996. X-ray and NMR structure of human Bcl-xL, an inhibitor of programmed cell death. Nature 381:335–341.
   PubMed Web of Science ®Google Scholar
• Nijhawan, D., M. Fang, E. Traer, Q. Zhong, W. Gao, F. Du, and X. Wang. 2003. Elimination of Mcl-1 is required for the initiation of apoptosis following ultraviolet irradiation. Genes Dev. 17:1475–1486.
   PubMed Web of Science ®Google Scholar
• Opferman, J. T., A. Letai, C. Beard, M. D. Sorcinelli, C. C. Ong, and S. J. Korsmeyer. 2003. Development and maintenance of B and T lymphocytes requires antiapoptotic MCL-1. Nature 426:671–676.
   PubMed Web of Science ®Google Scholar
• Reynolds, J. E., T. Yang, L. Qian, J. D. Jenkinson, P. Zhou, A. Eastman, and R. W. Craig. 1994. Mcl-1, a member of the Bcl-2 family, delays apoptosis induced by c-Myc overexpression in Chinese hamster ovary cells. Cancer Res. 54:6348–6352.
   PubMed Web of Science ®Google Scholar
• Rinkenberger, J. L., S. Horning, B. Klocke, K. Roth, and S. J. Korsmeyer. 2000. Mcl-1 deficiency results in peri-implantation embryonic lethality. Genes Dev. 14:23–27.
   PubMed Web of Science ®Google Scholar
• Thaw, P., N. J. Baxter, A. M. Hounslow, C. Price, J. P. Waltho, and C. J. Craven. 2001. Structure of TCTP reveals unexpected relationship with guanine nucleotide-free chaperones. Nat. Struct. Biol. 8:701–704.
   PubMedGoogle Scholar
• Tuynder, M., L. Susini, S. Prieur, S. Besse, G. Fiucci, R. Amson, and A. Telerman. 2002. Biological models and genes of tumor reversion: cellular reprogramming through tpt1/TCTP and SIAH-1. Proc. Natl. Acad. Sci. USA 99:14976–14981.
   PubMed Web of Science ®Google Scholar
• Wang, J. M., J. R. Chao, W. Chen, M. L. Kuo, J. J. Y. Yen, and H. F. Yang-Yen. 1999. The antiapoptotic gene mcl-1 is up-regulated by the phosphatidylinositol 3-kinase/Akt signaling pathway through a transcription factor complex containing CREB. Mol. Cell. Biol. 19:6195–6206.
   PubMed Web of Science ®Google Scholar
• Wang, J. M., M. J. Lai, and H. F. Yang-Yen. 2003. Interleukin-3 stimulation of mcl-1 gene transcription involves activation of the PU. 1 transcription factor through a p38 mitogen-activated protein kinase-dependent pathway. Mol. Cell. Biol. 23:1896–1909.
   PubMedGoogle Scholar
• Wang, K., A. Gross, G. Waksman, and S. J. Korsmeyer. 1998. Mutagenesis of the BH3 domain of BAX identifies residues critical for dimerization and killing. Mol. Cell. Biol. 18:6083–6089.
   PubMed Web of Science ®Google Scholar
• Yang, T., H. L. Buchan, K. J. Townsend, and R. W. Craig. 1996. MCL-1, a member of the BLC-2 family, is induced rapidly in response to signals for cell differentiation or death, but not to signals for cell proliferation. J. Cell Physiol. 166:523–536.
   PubMed Web of Science ®Google Scholar
• Yang, T., K. M. Kozopas, and R. W. Craig. 1995. The intracellular distribution and pattern of expression of Mcl-1 overlap with, but are not identical to, those of Bcl-2. J. Cell Biol. 128:1173–1184.
   PubMed Web of Science ®Google Scholar
• Yarm, F. R. 2002. Plk phosphorylation regulates the microtubule-stabilizing protein TCTP. Mol. Cell. Biol. 22:6209–6221.
   PubMed Web of Science ®Google Scholar
• Yenofsky, R., S. Cereghini, A. Krowczynska, and G. Brawerman. 1983. Regulation of mRNA utilization in mouse erythroleukemia cells induced to differentiate by exposure to dimethyl sulfoxide. Mol. Cell. Biol. 3:1197–1203.
   PubMedGoogle Scholar
• Zhang, D., F. Li, D. Weidner, Z. H. Mnjoyan, and K. Fujise. 2002. Physical and functional interaction between myeloid cell leukemia 1 protein (MCL1) and fortilin: the potential role of MCL1 as a fortilin chaperone. J. Biol. Chem. 277:37430–37438.
   PubMed Web of Science ®Google Scholar
• Zhou, P., L. Qian, K. M. Kozopas, and R. W. Craig. 1997. Mcl-1, a Bcl-2 family member, delays the death of hematopoietic cells under a variety of apoptosis-inducing conditions. Blood 89:630–643.
   PubMed Web of Science ®Google Scholar