Mcl-1 Integrates the Opposing Actions of Signaling Pathways That Mediate Survival and Apoptosis

REFERENCES

• Adams, K. W., and G. M. Cooper. 2007. Rapid turnover of Mcl-1 couples translation to cell survival and apoptosis. J. Biol. Chem. 282:6192–6200.
   PubMed Web of Science ®Google Scholar
• Badea, T. C., Y. Wang, and J. Nathans. 2003. A noninvasive genetic/pharmacologic strategy for visualizing cell morphology and clonal relationships in the mouse. J. Neurosci. 23:2314–2322.
   PubMedGoogle Scholar
• Brar, G. A., B. M. Kiburz, Y. Zhang, J. E. Kim, F. White, and A. Amon. 2006. Rec8 phosphorylation and recombination promote the step-wise loss of cohesins in meiosis. Nature 441:532–536.
   PubMed Web of Science ®Google Scholar
• Czabotar, P. E., E. F. Lee, M. F. van Delft, C. L. Day, B. J. Smith, D. C. Huang, W. D. Fairlie, M. G. Hinds, and P. M. Colman. 2007. Structural insights into the degradation of Mcl-1 induced by BH3 domains. Proc. Natl. Acad. Sci. USA 104:6217–6222.
   PubMed Web of Science ®Google Scholar
• Das, M., F. Jiang, H. K. Sluss, C. Zhang, K. M. Shokat, R. A. Flavell, and R. J. Davis. 2007. Suppression of p53-dependent senescence by the JNK signal transduction pathway. Proc. Natl. Acad. Sci. USA 104:15759–15764.
   PubMed Web of Science ®Google Scholar
• Davis, R. J. 2000. Signal transduction by the JNK group of MAP kinases. Cell 103:239–252.
   PubMed Web of Science ®Google Scholar
• Ding, Q., X. He, J. M. Hsu, W. Xia, C. T. Chen, L. Y. Li, D. F. Lee, J. C. Liu, Q. Zhong, X. Wang, and M. C. Hung. 2007. Degradation of Mcl-1 by beta-TrCP mediates glycogen synthase kinase 3-induced tumor suppression and chemosensitization. Mol. Cell. Biol. 27:4006–4017.
   PubMedGoogle Scholar
• Doble, B. W., and J. R. Woodgett. 2003. GSK-3: tricks of the trade for a multi-tasking kinase. J. Cell Sci. 116:1175–1186.
   PubMed Web of Science ®Google Scholar
• Domina, A. M., J. A. Vrana, M. A. Gregory, S. R. Hann, and R. W. Craig. 2004. MCL1 is phosphorylated in the PEST region and stabilized upon ERK activation in viable cells, and at additional sites with cytotoxic okadaic acid or taxol. Oncogene 23:5301–5315.
   PubMed Web of Science ®Google Scholar
• Dong, C., D. D. Yang, M. Wysk, A. J. Whitmarsh, R. J. Davis, and R. A. Flavell. 1998. Defective T cell differentiation in the absence of Jnk1. Science 282:2092–2095.
   PubMed Web of Science ®Google Scholar
• Fritsch, R. M., G. Schneider, D. Saur, M. Scheibel, and R. M. Schmid. 2007. Translational repression of MCL-1 couples stress-induced eIF2 alpha phosphorylation to mitochondrial apoptosis initiation. J. Biol. Chem. 282:22551–22562.
   PubMedGoogle Scholar
• He, X., J. P. Saint-Jeannet, J. R. Woodgett, H. E. Varmus, and I. B. Dawid. 1995. Glycogen synthase kinase-3 and dorsoventral patterning in Xenopus embryos. Nature 374:617–622.
   PubMedGoogle Scholar
• Herrant, M., A. Jacquel, S. Marchetti, N. Belhacene, P. Colosetti, F. Luciano, and P. Auberger. 2004. Cleavage of Mcl-1 by caspases impaired its ability to counteract Bim-induced apoptosis. Oncogene 23:7863–7873.
   PubMed Web of Science ®Google Scholar
• Hubner, A., T. Barrett, R. A. Flavell, and R. J. Davis. 2008. Multisite phosphorylation regulates Bim stability and apoptotic activity. Mol. Cell 30:415–425.
   PubMed Web of Science ®Google Scholar
• Inoshita, S., K. Takeda, T. Hatai, Y. Terada, M. Sano, J. Hata, A. Umezawa, and H. Ichijo. 2002. Phosphorylation and inactivation of myeloid cell leukemia 1 by JNK in response to oxidative stress. J. Biol. Chem. 277:43730–43734.
   PubMed Web of Science ®Google Scholar
• Jaeschke, A., M. Karasarides, J. J. Ventura, A. Ehrhardt, C. Zhang, R. A. Flavell, K. M. Shokat, and R. J. Davis. 2006. JNK2 is a positive regulator of the cJun transcription factor. Mol. Cell 23:899–911.
   PubMed Web of Science ®Google Scholar
• Kennedy, N. J., H. K. Sluss, S. N. Jones, D. Bar-Sagi, R. A. Flavell, and R. J. Davis. 2003. Suppression of Ras-stimulated transformation by the JNK signal transduction pathway. Genes Dev. 17:629–637.
   PubMed Web of Science ®Google Scholar
• Kobayashi, S., S. H. Lee, X. W. Meng, J. L. Mott, S. F. Bronk, N. W. Werneburg, R. W. Craig, S. H. Kaufmann, and G. J. Gores. 2007. Serine 64 phosphorylation enhances the antiapoptotic function of Mcl-1. J. Biol. Chem. 282:18407–18417.
   PubMedGoogle Scholar
• Lamb, J. A., J. J. Ventura, P. Hess, R. A. Flavell, and R. J. Davis. 2003. JunD mediates survival signaling by the JNK signal transduction pathway. Mol. Cell 11:1479–1489.
   PubMed Web of Science ®Google Scholar
• Liu, H., H. W. Peng, Y. S. Cheng, H. S. Yuan, and H. F. Yang-Yen. 2005. Stabilization and enhancement of the antiapoptotic activity of mcl-1 by TCTP. Mol. Cell. Biol. 25:3117–3126.
   PubMed Web of Science ®Google Scholar
• Maurer, U., C. Charvet, A. S. Wagman, E. Dejardin, and D. R. Green. 2006. Glycogen synthase kinase-3 regulates mitochondrial outer membrane permeabilization and apoptosis by destabilization of MCL-1. Mol. Cell 21:749–760.
   PubMed Web of Science ®Google Scholar
• Michels, J., J. W. O'Neill, C. L. Dallman, A. Mouzakiti, F. Habens, M. Brimmell, K. Y. Zhang, R. W. Craig, E. G. Marcusson, P. W. Johnson, and G. Packham. 2004. Mcl-1 is required for Akata6 B-lymphoma cell survival and is converted to a cell death molecule by efficient caspase-mediated cleavage. Oncogene 23:4818–4827.
   PubMed Web of Science ®Google Scholar
• Moser, K., and F. M. White. 2006. Phosphoproteomic analysis of rat liver by high capacity IMAC and LC-MS/MS. J. Proteome Res. 5:98–104.
   PubMedGoogle Scholar
• Mott, J. L., S. Kobayashi, S. F. Bronk, and G. J. Gores. 2007. mir-29 regulates Mcl-1 protein expression and apoptosis. Oncogene 26:6133–6140.
   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. 2007. Life and death during hematopoietic differentiation. Curr. Opin. Immunol. 19:497–502.
   PubMed Web of Science ®Google Scholar
• Opferman, J. T. 2006. Unraveling MCL-1 degradation. Cell Death Differ. 13:1260–1262.
   PubMed Web of Science ®Google Scholar
• Opferman, J. T., H. Iwasaki, C. C. Ong, H. Suh, S. Mizuno, K. Akashi, and S. J. Korsmeyer. 2005. Obligate role of anti-apoptotic MCL-1 in the survival of hematopoietic stem cells. Science 307:1101–1104.
   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
• 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
• Tournier, C., P. Hess, D. D. Yang, J. Xu, T. K. Turner, A. Nimnual, D. Bar-Sagi, S. N. Jones, R. A. Flavell, and R. J. Davis. 2000. Requirement of JNK for stress-induced activation of the cytochrome c-mediated death pathway. Science 288:870–874.
   PubMed Web of Science ®Google Scholar
• Viatour, P., E. Dejardin, M. Warnier, F. Lair, E. Claudio, F. Bureau, J. C. Marine, M. P. Merville, U. Maurer, D. Green, J. Piette, U. Siebenlist, V. Bours, and A. Chariot. 2004. GSK3-mediated BCL-3 phosphorylation modulates its degradation and its oncogenicity. Mol. Cell 16:35–45.
   PubMedGoogle Scholar
• Weston, C. R., and R. J. Davis. 2001. Signal transduction: signaling specificity—a complex affair. Science 292:2439–2440.
   PubMedGoogle Scholar
• Weston, C. R., and R. J. Davis. 2007. The JNK signal transduction pathway. Curr. Opin. Cell Biol. 19:142–149.
   PubMed Web of Science ®Google Scholar
• Whitmarsh, A. J., and R. J. Davis. 2001. Analyzing JNK and p38 mitogen-activated protein kinase activity. Methods Enzymol. 332:319–336.
   PubMedGoogle Scholar
• Willis, S. N., L. Chen, G. Dewson, A. Wei, E. Naik, J. I. Fletcher, J. M. Adams, and D. C. Huang. 2005. Proapoptotic Bak is sequestered by Mcl-1 and Bcl-xL, but not Bcl-2, until displaced by BH3-only proteins. Genes Dev. 19:1294–1305.
   PubMed Web of Science ®Google Scholar
• Xia, Z., M. Dickens, J. Raingeaud, R. J. Davis, and M. E. Greenberg. 1995. Opposing effects of ERK and JNK-p38 MAP kinases on apoptosis. Science 270:1326–1331.
   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
• Zhong, Q., W. Gao, F. Du, and X. Wang. 2005. Mule/ARF-BP1, a BH3-only E3 ubiquitin ligase, catalyzes the polyubiquitination of Mcl-1 and regulates apoptosis. Cell 121:1085–1095.
   PubMed Web of Science ®Google Scholar