Ubiquitination and Degradation of ATF2 Are Dimerization Dependent

REFERENCES

• Abdel-Hafiz, H. A., C. Y. Chen, T. Marcell, D. J. Kroll, and J. Hoeffler 1993. Structural determinants outside of the leucine zipper influence the interactions of CREB and ATF-2: interaction of CREB with ATF-2 blocks E1a-ATF-2 complex formation. Oncogene 8:1161–1174.
   PubMedGoogle Scholar
• Benbrook, D. M., and J. Jones 1990. Heterodimer formation between CREB and JUN proteins. Oncogene 5:295–302.
   PubMed Web of Science ®Google Scholar
• Bocco, J. L., A. Bahr, J. Goetz, C. Hauss, T. Kallunki, C. Kedinger, and J. Chatton 1996. In vivo association of ATFa with JNK/SAP kinase activities. Oncogene 12:1971–1980.
   PubMedGoogle Scholar
• Deng, T., and J. Karin 1993. JunB differs from c-Jun in its DNA-binding and dimerization domains, and represses c-Jun by formation of inactive heterodimers. Genes Dev. 7:479–490.
   PubMed Web of Science ®Google Scholar
• Firestein, R., and J. Feuerstein 1998. Association of activating transcription factor 2 (ATF2) with the ubiquitin-conjugating enzyme hUBC9. Implication of the ubiquitin/proteasome pathway in regulation of ATF2 in T cells. J. Biol. Chem. 273:5892–5902.
   PubMedGoogle Scholar
• Fuchs, S. Y., L. Dolan, R. J. Davis, and J. Ronai 1996. Phosphorylation-dependent targeting of c-Jun ubiquitination by Jun N-kinase. Oncogene 13:1531–1535.
   PubMedGoogle Scholar
• Fuchs, S. Y., B. Xie, V. Adler, V. A. Fried, R. J. Davis, and J. Ronai 1997. c-Jun NH2-terminal kinases target the ubiquitination of their associated transcription factors. J. Biol. Chem. 272:32163–32168.
   PubMed Web of Science ®Google Scholar
• Fuchs, S. Y., V. Adler, T. Buschmann, Z. Yin, X. Wu, S. N. Jones, and J. Ronai 1998. JNK targets p53 ubiquitination and degraduation in nonstressed cells. Genes Dev. 12:2658–2663.
   PubMed Web of Science ®Google Scholar
• Fuchs, S. Y., V. A. Fried, and J. Ronai 1998. Stress-activated kinases regulate protein stability. Oncogene 17:1483–1490.
   PubMedGoogle Scholar
• Georgopoulos, K., B. A. Morgan, and J. Moore 1992. Functionally distinct isoforms of the CRE-BP DNA-binding protein mediate activity of a T-cell-specific enhancer. Mol. Cell. Biol. 12:747–757.
   PubMedGoogle Scholar
• Gupta, S., D. Campbell, B. Derijard, and J. Davis 1995. Transcription factor ATF2 regulation by the JNK signal transduction pathway. Science 267:389–393.
   PubMed Web of Science ®Google Scholar
• Gupta, S., T. Barrett, A. J. Whitmarsh, J. Cavanagh, H. K. Sluss, B. Derijard, and J. Davis 1996. Selective interaction of JNK protein kinase isoforms with transcription factors. EMBO J. 15:2760–2770.
   PubMed Web of Science ®Google Scholar
• Hai, T. W., F. Liu, W. J. Coukos, and J. Green 1989. Transcription factor ATF cDNA clones: an extensive family of leucine zipper proteins able to selectively form DNA-binding heterodimers. Genes Dev. 3:2083–2090.
   PubMed Web of Science ®Google Scholar
• Hoeffler, J. P. 1992. Structure/function relationships of CREB/ATF proteins. J. Investig. Dermatol. 98:21S–28S.
   PubMedGoogle Scholar
• Ivanov, V., and Z. Ronai. Downregulation of TNFα expression by ATF2 increases UVC-induced apoptosis of late stage melanoma cells. J. Biol. Chem., in press.
   Google Scholar
• Kallunki, T., T. Deng, M. Hibi, and J. Karin 1996. c-Jun can recruit JNK to phosphorylate dimerization partners via specific docking interactions. Cell 87:929–939.
   PubMedGoogle Scholar
• Karin, M., and J. Hunter 1995. Transcriptional control by protein phosphorylation: signal transmission from the cell surface to the nucleus. Curr. Biol. 5:747–757.
   PubMed Web of Science ®Google Scholar
• Kim, S. J., S. Wagner, F. Liu, M. A. O’Reilly, P. D. Robbins, and J. Green 1992. Retinoblastoma gene product activates expression of the human TGF-beta 2 gene through transcription factor ATF-2. Nature 358:331–334.
   PubMed Web of Science ®Google Scholar
• Li, X. Y., and J. Green 1996. Intramolecular inhibition of activating transcription factor-2 function by its DNA-binding domain. Genes Dev. 10:517–527.
   PubMed Web of Science ®Google Scholar
• Lin, A., A. Minden, H. Martinetto, F. X. Claret, C. Lange-Carter, F. Mercurio, G. L. Johnson, and J. Karin 1995. Identification of a dual specificity kinase that activates the Jun kinases and p38-Mpk2. Science 268:286–290.
   PubMed Web of Science ®Google Scholar
• Liu, F., and J. Green 1990. A specific member of the ATF transcription factor family can mediate transcription activation by the adenovirus E1a protein. Cell 61:1217–1224.
   PubMed Web of Science ®Google Scholar
• Liu, F., and J. Green 1994. Promoter targeting by adenovirus E1a through interaction with different cellular DNA-binding domains. Nature 368:520–525.
   PubMedGoogle Scholar
• Livingstone, C., G. Patel, and J. Jones 1995. ATF-2 contains a phosphorylation-dependent transcriptional activation domain. EMBO J. 14:1785–1797.
   PubMed Web of Science ®Google Scholar
• Maekawa, T., H. Sakura, C. Kanei-Isheii, T. Sudo, T. Yoshimora, J. Fijisawa, M. Yoshida, and J. Ishii 1989. Leucine zipper structure of the protein CRE-BP1 binding to the cAMP response element in brain. EMBO J. 8:2023–2028.
   PubMed Web of Science ®Google Scholar
• Maguire, H. F., J. P. Hoeffler, and J. Siddiqui 1991. HBV X protein alters the DNA binding specificity of CREB and ATF-2 by protein-protein interactions. Science 252:842–844.
   PubMed Web of Science ®Google Scholar
• Minden, A., A. Lin, M. McMahon, C. Lange-Carter, B. Derijard, R. J. Davis, G. L. Johnson, and J. Karin 1994. Differential activation of ERK and JNK mitogen-activated protein kinases by Raf-1 and MEKK. Science 266:1719–1723.
   PubMed Web of Science ®Google Scholar
• Narayan, S., S. G. Widen, W. A. Beard, and J. Wilson 1994. RNA polymerase II transcription. Rate of promoter clearance is enhanced by a purified activating transcription factor/cAMP response element-binding protein. J. Biol. Chem. 269:12755–12763.
   PubMedGoogle Scholar
• Papavassiliou, A. G., M. Treier, C. Chavrier, and J. Bohmann 1994. Targeted degradation of c-Fos, but not v-Fos, by a phosphorylation-dependent signal on c-Jun. Science 258:1941–1944.
   Google Scholar
• Pfarr, C. M., F. Mechta, G. Spyrou, D. Lallemand, S. Carillo, and J. Yaniv 1994. Mouse JunD negatively regulates fibroblast growth and antagonizes transformation by ras. Cell 76:747–760.
   PubMedGoogle Scholar
• Raingeaud, J., A. J. Whitmarsh, T. Barrett, B. Derijard, and J. Davis 1996. MKK3- and MKK6-regulated gene expression is mediated by the p38 mitogen-activated protein kinase signal transduction pathway. Mol. Cell. Biol. 16:1247–1255.
   PubMed Web of Science ®Google Scholar
• Read, M. A., M. Z. Whitley, S. Gupta, J. W. Pierce, J. Best, R. J. Davis, and J. Collins 1997. Tumor necrosis factor alpha-induced E-selectin expression is activated by the nuclear factor-kappaB and c-JUN N-terminal kinase/p38 mitogen-activated protein kinase pathways. J. Biol. Chem. 272:2753–2761.
   PubMed Web of Science ®Google Scholar
• Ronai, Z., Y. M. Yang, S. Y. Fuchs, V. Adler, M. Sardana, and J. Herlyn 1998. ATF2 confers radiation resistance to human melanoma cells. Oncogene 16:523–531.
   PubMedGoogle Scholar
• Shimizu, M., Y. Nomura, H. Suzuki, E. Ichikawa, A. Takeuchi, M. Suzuki, T. Nakamura, T. Nakajima, and J. Oda 1998. Activation of the rat cyclin A promoter by ATF2 and Jun family members and its suppression by ATF4. Exp. Cell Res. 239:93–103.
   PubMedGoogle Scholar
• Stancovski, I., H. Gonen, A. Orian, A. L. Schwartz, and J. Ciechanover 1995. Degradation of the proto-oncogene product c-Fos by the ubiquitin proteolytic system in vivo and in vitro: identification and characterization of the conjugating enzymes. Mol. Cell. Biol. 15:7106–7116.
   PubMed Web of Science ®Google Scholar
• Treier, M., L. M. Staszewski, and J. Bohmann 1994. Ubiquitin-dependent c-Jun degradation in vivo is mediated by the δ domain. Cell 78:787–798.
   PubMed Web of Science ®Google Scholar
• Tsai, E. Y., J. Jain, P. A. Pesavento, A. Rao, and J. Goldfeld 1996. Tumor necrosis factor alpha gene regulation in activated T cells involves ATF-2/Jun and NFATp. Mol. Cell. Biol. 16:459–467.
   PubMedGoogle Scholar
• van Dam, H., M. Duyndam, R. Rottier, A. Bosch, L. de Vries-Smits, P. Herrlich, A. Zantema, P. Angel, and J. van der Eb 1993. Heterodimer formation of cJun and ATF-2 is responsible for induction of c-jun by the 243 amino acid adenovirus E1A protein. EMBO J. 12:479–487.
   PubMed Web of Science ®Google Scholar
• van Dam, H., D. Wilhelm, I. Herr, A. Steffen, P. Herrlich, and J. Angel 1995. ATF-2 is preferentially activated by stress-activated protein kinases to mediate c-jun induction in response to genotoxic agents. EMBO J. 14:1798–1811.
   PubMed Web of Science ®Google Scholar
• van Dam, H., S. Huguier, K. Kooistra, J. Baguet, E. Vial, A. J. van der Eb, P. Herrlich, P. Angel, and J. Castellazzi 1998. Autocrine growth and anchorage independence: two complementing Jun-controlled genetic programs of cellular transformation. Genes Dev. 12:1227–1239.
   PubMedGoogle Scholar
• Wagner, S., and J. Green 1993. HTLV-I Tax protein stimulation of DNA binding of bZIP proteins by enhancing dimerization. Science 262:395–399.
   PubMed Web of Science ®Google Scholar
• Wagner, S., and J. Green 1994. DNA-binding domains: targets for viral and cellular regulators. Curr. Opin. Cell Biol. 6:410–414.
   PubMed Web of Science ®Google Scholar
• Yang-Yen, H. F., R. Chiu, and J. Karin 1990. Elevation of AP1 activity during F9 cell differentiation is due to increased c-jun transcription. New Biol. 2:351–361.
   PubMedGoogle Scholar