The N and C Termini of the Splice Variants of the Human Mitogen-Activated Protein Kinase-Interacting Kinase Mnk2 Determine Activity and Localization

REFERENCES

• Borden, K. L. 2000. RING domains: master builders of molecular scaffolds? J. Mol. Biol. 295: 1103–1112.
   PubMedGoogle Scholar
• Cohen, N., M. Sharma, A. Kentsis, J. M. Perez, S. Strudwick, and K. L. Borden. 2001. PML RING suppresses oncogenic transformation by reducing the affinity of eIF4E for mRNA. EMBO J. 20: 4547–4559.
   PubMed Web of Science ®Google Scholar
• Dahlberg, J. E., E. Lund, and E. B. Goodwin. 2003. Nuclear translation: what is the evidence? RNA 9: 1–8.
   PubMedGoogle Scholar
• De Benedetti, A., and R. E. Rhoads. 1990. Overexpression of eukaryotic protein synthesis initiation factor 4E in HeLa cells results in aberrant growth and morphology. Proc. Natl. Acad. Sci. USA 87: 8212–8216.
   PubMed Web of Science ®Google Scholar
• Dostie, J., M. Ferraiuolo, A. Pause, S. A. Adam, and N. Sonenberg. 2000. A novel shuttling protein, 4E-T, mediates the nuclear import of the mRNA 5′ cap-binding protein, eIF4E. EMBO J. 19: 3142–3156.
   PubMedGoogle Scholar
• Dostie, J., F. Lejbkowicz, and N. Sonenberg. 2000. Nuclear eukaryotic initiation factor 4E (eIF4E) colocalizes with splicing factors in speckles. J. Cell Biol. 148: 239–247.
   PubMed Web of Science ®Google Scholar
• Flynn, A., and C. G. Proud. 1995. Serine 209, not serine 53, is the major site of phosphorylation in initiation factor eIF-4E in serum-treated Chinese hamster ovary cells. J. Biol. Chem. 270: 21684–21688.
   PubMed Web of Science ®Google Scholar
• Flynn, A., R. G. Vries, and C. G. Proud. 1997. Signalling pathways which regulate eIF4E. Biochem. Soc. Trans. 25: 192S.
   PubMed Web of Science ®Google Scholar
• Fukunaga, R., and T. Hunter. 1997. MNK1, a new MAP kinase-activated protein kinase, isolated by a novel expression screening method for identifying protein kinase substrates. EMBO J. 16: 1921–1933.
   PubMed Web of Science ®Google Scholar
• Gingras, A.-C., B. Raught, and N. Sonenberg. 1999. eIF4 initiation factors: effectors of mRNA recruitment to ribosomes and regulators of translation. Annu. Rev. Biochem. 68: 913–963.
   PubMed Web of Science ®Google Scholar
• Hunter, T. 1994. 1001 protein kinases redux—towards 2000. Semin. Cell. Biol. 5: 367–376.
   PubMedGoogle Scholar
• Iborra, F. J., D. A. Jackson, and P. R. Cook. 2001. Coupled transcription and translation within nuclei of mammalian cells. Science 293: 1139–1142.
   PubMed Web of Science ®Google Scholar
• Jans, D. A., C. Y. Xiao, and M. H. Lam. 2000. Nuclear targeting signal recognition: a key control point in nuclear transport? Bioessays 22: 532–544.
   PubMed Web of Science ®Google Scholar
• Joel, P. B., J. Smith, T. W. Sturgill, T. L. Fisher, J. Blenis, and D. A. Lannigan. 1998. pp90rsk1 regulates estrogen receptor-mediated transcription through phosphorylation of Ser-167. Mol. Cell. Biol. 18: 1978–1984.
   PubMed Web of Science ®Google Scholar
• Joshi, B., A. L. Cai, B. D. Keiper, W. B. Minich, R. Mendez, C. M. Beach, J. Stepinski, R. Stolarski, E. Darzynkiewicz, and R. E. Rhoads. 1995. Phosphorylation of eukaryotic protein synthesis initiation factor 4E at Ser-209. J. Biol. Chem. 270: 14597–14603.
   PubMed Web of Science ®Google Scholar
• Kleijn, M., G. C. Scheper, M. L. Wilson, A. R. Tee, and C. G. Proud. 2002. Localisation and regulation of the eIF4E-binding protein 4E-BP3. FEBS Lett. 532: 319–323.
   PubMedGoogle Scholar
• Kleijn, M., H. O. Voorma, and A. A. M. Thomas. 1995. Phosphorylation of eIF-4E and initiation of protein synthesis in P19 embryonal carcinoma cells. J. Cell. Biochem. 59: 443–452.
   PubMedGoogle Scholar
• Lai, H. K., and K. L. Borden. 2000. The promyelocytic leukemia (PML) protein suppresses cyclin D1 protein production by altering the nuclear cytoplasmic distribution of cyclin D1 mRNA. Oncogene 19: 1623–1634.
   PubMed Web of Science ®Google Scholar
• Lazaris-Karatzas, A., K. S. Montine, and N. Sonenberg. 1990. Malignant transformation by a eukaryotic initiation factor subunit that binds to mRNA 5′ cap. Nature 345: 544–547.
   PubMed Web of Science ®Google Scholar
• Lejbkowicz, F., C. Goyer, A. Darveau, S. Neron, R. Lemieux, and N. Sonenberg. 1992. A fraction of the mRNA 5′ cap-binding protein, eukaryotic initiation factor 4E, localizes to the nucleus. Proc. Natl. Acad. Sci. USA 89: 9612–9616.
   PubMed Web of Science ®Google Scholar
• Li, B. D., L. Liu, M. Dawson, and A. De Benedetti. 1997. Overexpression of eukaryotic initiation factor 4E (eIF4E) in breast carcinoma. Cancer 79: 2385–2390.
   PubMed Web of Science ®Google Scholar
• Li, W., G. J. Belsham, and C. G. Proud. 2001. Eukaryotic initiation factors 4A (eIF4A) and 4G (eIF4G) mutually interact in a 1:1 ratio in vivo. J. Biol. Chem. 276: 29111–29115.
   PubMedGoogle Scholar
• McKendrick, L., E. Thompson, J. Ferreira, S. J. Morley, and J. D. Lewis. 2001. Interaction of eukaryotic translation initiation factor 4G with the nuclear cap-binding complex provides a link between nuclear and cytoplasmic functions of the m7 guanosine cap. Mol. Cell. Biol. 21: 3632–3641.
   PubMed Web of Science ®Google Scholar
• Meng, W., L. L. Swenson, M. J. Fitzgibbon, K. Hayakawa, E. Ter Haar, A. E. Behrens, J. R. Fulghum, and J. A. Lippke. 2002. Structure of mitogen-activated protein kinase-activated protein (MAPKAP) kinase 2 suggests a bifunctional switch that couples kinase activation with nuclear export. J. Biol. Chem. 277: 37401–37405.
   PubMedGoogle Scholar
• Minich, W. B., M. L. Balasta, D. J. Goss, and R. E. Rhoads. 1994. Chromatographic resolution of in vivo phosphorylated and nonphosphorylated eukaryotic translation initiation factor eIF-4E: increased cap affinity of the phosphorylated form. Proc. Natl. Acad. Sci. USA 91: 7668–7672.
   PubMed Web of Science ®Google Scholar
• Morley, S. J., and L. McKendrick. 1997. Involvement of stress-activated protein kinase and p38/RK mitogen-activated protein kinase signaling pathways in the enhanced phosphorylation of initiation factor 4E in NIH 3T3 cells. J. Biol. Chem. 272: 17887–17893.
   PubMed Web of Science ®Google Scholar
• Nathan, C. A., S. Franklin, F. W. Abreo, R. Nassar, A. De Benedetti, and J. Glass. 1999. Analysis of surgical margins with the molecular marker eIF4E: a prognostic factor in patients with head and neck cancer. J. Clin. Oncol. 17: 2909–2914.
   PubMed Web of Science ®Google Scholar
• Nathanson, L., T. Xia, and M. P. Deutscher. 2003. Nuclear protein synthesis: a re-evaluation. RNA 9: 9–13.
   PubMedGoogle Scholar
• Pyronnet, S., H. Imataka, A. C. Gingras, R. Fukunaga, T. Hunter, and N. Sonenberg. 1999. Human eukaryotic translation initiation factor 4G (eIF4G) recruits Mnk1 to phosphorylate eIF4E. EMBO J. 18: 270–279.
   PubMed Web of Science ®Google Scholar
• Raught, B., A. C. Gingras, S. P. Gygi, H. Imataka, S. Morino, A. Gradi, R. Aebersold, and N. Sonenberg. 2000. Serum-stimulated, rapamycin-sensitive phosphorylation sites in the eukaryotic translation initiation factor 4GI. EMBO J. 19: 434–444.
   PubMed Web of Science ®Google Scholar
• Sanz, V., I. Arozarena, and P. Crespo. 2000. Distinct carboxy-termini confer divergent characteristics to the mitogen-activated protein kinase p38α and its splice isoform Mxi2. FEBS Lett. 474: 169–174.
   PubMedGoogle Scholar
• Scheper, G. C., N. A. Morrice, M. Kleijn, and C. G. Proud. 2001. The mitogen-activated protein kinase signal-integrating kinase Mnk2 is a eukaryotic initiation factor 4E kinase with high levels of basal activity in mammalian cells. Mol. Cell. Biol. 21: 743–754.
   PubMed Web of Science ®Google Scholar
• Scheper, G. C., and C. G. Proud. 2002. Does phosphorylation of the cap-binding protein eIF4E play a role in translation initiation? Eur. J. Biochem. 269: 5350–5359.
   PubMedGoogle Scholar
• Scheper, G. C., B. van Kollenburg, J. Hu, Y. Luo, D. J. Goss, and C. G. Proud. 2002. Phosphorylation of eukaryotic initiation factor 4E markedly reduces its affinity for capped mRNA. J. Biol. Chem. 277: 3303–3309.
   PubMed Web of Science ®Google Scholar
• Scheper, G. C., R. van Wijk, and A. A. M. Thomas. 2001. Regulation of the activity of eukaryotic initiation factors in stressed cells, p. 39–52. In R. E. Rhoads (ed.), Signaling pathways for translation. Springer-Verlag, Berlin, Germany.
   Google Scholar
• Seternes, O. M., B. Johansen, B. Hegge, M. Johannessen, S. M. Keyse, and U. Moens. 2002. Both binding and activation of p38 mitogen-activated protein kinase (MAPK) play essential roles in regulation of the nucleocytoplasmic distribution of MAPK-activated protein kinase 5 by cellular stress. Mol. Cell. Biol. 22: 6931–6945.
   PubMedGoogle Scholar
• Slentz-Kesler, K., J. T. Moore, M. Lombard, J. Zhang, R. Hollingsworth, and M. P. Weiner. 2000. Identification of the human mnk2 gene (MKNK2) through protein interaction with estrogen receptor beta. Genomics 69: 63–71.
   PubMed Web of Science ®Google Scholar
• Smith, J. A., C. E. Poteet-Smith, D. A. Lannigan, T. A. Freed, A. J. Zoltoski, and T. W. Sturgill. 2000. Creation of a stress-activated p90 ribosomal S6 kinase. The carboxyl-terminal tail of the MAPK-activated protein kinases dictates the signal transduction pathway in which they function. J. Biol. Chem. 275: 31588–31593.
   PubMedGoogle Scholar
• Smith, J. A., C. E. Poteet-Smith, K. Malarkey, and T. W. Sturgill. 1999. Identification of an extracellular signal-regulated kinase (ERK) docking site in ribosomal S6 kinase, a sequence critical for activation by ERK in vivo. J. Biol. Chem. 274: 2893–2898.
   PubMed Web of Science ®Google Scholar
• Smith, M. R., M. Jaramillo, Y. L. Liu, T. E. Dever, W. C. Merrick, H. F. Kung, and N. Sonenberg. 1990. Translation initiation factors induce DNA synthesis and transform NIH 3T3 cells. New Biol. 2: 648–654.
   PubMedGoogle Scholar
• Sonenberg, N., M. A. Morgan, W. C. Merrick, and A. J. Shatkin. 1978. A polypeptide in eukaryotic initiation factors that crosslinks specifically to the 5′-terminal cap in mRNA. Proc. Natl. Acad. Sci. USA 75: 4843–4847.
   PubMed Web of Science ®Google Scholar
• Stern, B. D., M. Wilson, and R. Jagus. 1993. Use of nonreducing SDS-PAGE for monitoring renaturation of recombinant protein synthesis initiation factor, eIF-4α. Protein Expr. Purif. 4: 320–327.
   PubMed Web of Science ®Google Scholar
• Strudwick, S., and K. L. Borden. 2002. The emerging roles of translation factor eIF4E in the nucleus. Differentiation 70: 10–22.
   PubMed Web of Science ®Google Scholar
• Stuurman, N., A. de Graaf, A. Floore, A. Josso, B. Humbel, L. de Jong, and R. van Driel. 1992. A monoclonal antibody recognizing nuclear matrix-associated nuclear bodies. J. Cell Sci. 101: 773–784.
   PubMed Web of Science ®Google Scholar
• Tournier, C., A. J. Whitmarsh, J. Cavanagh, T. Barrett, and R. J. Davis. 1997. Mitogen-activated protein kinase kinase 7 is an activator of the c-Jun NH2-terminal kinase. Proc. Natl. Acad. Sci. USA 94: 7337–7342.
   PubMed Web of Science ®Google Scholar
• Tschopp, C., U. Knauf, M. Brauchle, M. Zurini, P. Ramage, D. Glueck, L. New, J. Han, and H. Gram. 2000. Phosphorylation of eIF-4E on Ser 209 in response to mitogenic and inflammatory stimuli is faithfully detected by specific antibodies. Mol. Cell. Biol. Res. Commun. 3: 205–211.
   PubMedGoogle Scholar
• Wang, X., A. Flynn, A. J. Waskiewicz, B. L. Webb, R. G. Vries, I. A. Baines, J. A. Cooper, and C. G. Proud. 1998. The phosphorylation of eukaryotic initiation factor eIF4E in response to phorbol esters, cell stresses, and cytokines is mediated by distinct MAP kinase pathways. J. Biol. Chem. 273: 9373–9377.
   PubMed Web of Science ®Google Scholar
• Waskiewicz, A. J., A. Flynn, C. G. Proud, and J. A. Cooper. 1997. Mitogen-activated protein kinases activate the serine/threonine kinases Mnk1 and Mnk2. EMBO J. 16: 1909–1920.
   PubMed Web of Science ®Google Scholar
• Waskiewicz, A. J., J. C. Johnson, B. Penn, M. Mahalingam, S. R. Kimball, and J. A. Cooper. 1999. Phosphorylation of the cap-binding protein eukaryotic translation initiation factor 4E by protein kinase Mnk1 in vivo. Mol. Cell. Biol. 19: 1871–1880.
   PubMed Web of Science ®Google Scholar