Skip to main content
SpringerLink
Log in

Multiple Phosphorylation Sites and Quaternary Organization of Guanine-Nucleotide Exchange Complex of Elongation Factor-1 (EF-1βγδ/ValRS) Control the Various Functions of EF-1α

  • Published:
Bioscience Reports

Abstract

The eukaryotic guanine-nucleotide exchange factor commonly called elongation factor-1βγδ (EF-1βγδ), comprises four different subunits including valyl-tRNA synthetase (EF-1βγδ/ValRS). The factor is multiply-phosphorylated by three different protein kinases, protein kinase C, casein kinase II and cyclin dependent kinase 1 (CDK1). EF-1βγδ/ValRS is organized as a macromolecular complex for which we propose a new structural model. Evidence that EF-1βγδ/ValRS is a sophisticated supramolecular complex containing many phosphorylation sites, makes it a potential regulator of any of the functions of its partner EF-1α, not only involved in protein synthesis elongation, but also in many other cellular functions.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Similar content being viewed by others

REFERENCES

  • Bec, G. and Waller, J.-P. (1989) J. Biol. Chem. 264:21138–21143.

    Google Scholar 

  • Bec, G., Kerjan, P., and Waller, J. P. (1994) J. Biol. Chem. 269:2086–2092.

    Google Scholar 

  • Bellé, R., Derancourt, J., Poulhe, R., Capony, J. P., Ozon, R., and Mulner-Lorillon, O. (1989) Febs Lett. 255:101–104.

    Google Scholar 

  • Bellé, R., Minella, O., Morales, J., Cormier, P., Poulhe, R., and Mulner-Lorillon, O. (1995) in Progress in Cell Cycle Research (Meijer, L., Guidet, S., and Tung, H. Y. L., Eds.), vol. 1, Plenum Press, New York, pp. 265–270.

    Google Scholar 

  • Bourne, H. R. and Stryer, L. (1992) Nature 358:541–543.

    Google Scholar 

  • Brandsma, M., Kerjan, P., Dijk, J., Janssen, M. C., and Moller, W. (1995) Eur. J. Biochem. 233:277–282.

    Google Scholar 

  • Chi, K., Jones, D. V., and Frazier, M. L. (1992) Gastroenterology 103:98–102.

    Google Scholar 

  • Cormier, P., Osborne, H. B., Morales, J., Bassez, T., Minella, O., Poulhe, R., Bellé, R., and Mulner-Lorillon, O. (1993) Nucl. Acids Res. 21:743.

    Google Scholar 

  • Dinman, J. D. and Kinzy, T. G. (1997) RNA 3:870–881.

    Google Scholar 

  • Hershey, J. W. B. (1991) Annu. Rev. Biochem. 60:717–755.

    Google Scholar 

  • Janssen, G. M. C. and Moller, W. (1988a) Eur J. Biochem. 171:119–129.

    Google Scholar 

  • Janssen, G. M. C. and Moller, W. (1988b) J. Biol. Chem. 263:1773–1778.

    Google Scholar 

  • Janssen, G. M. C., Maessen, G. D. F., Amons, R., and Moller, W. (1988) J. Biol. Chem. 263:11063–11066.

    Google Scholar 

  • Janssen, G. M. C., Morales, J., Schipper, A., Mulner-Lorillon, O., Bellé, R., and Moller, W. (1991) J. Biol. Chem. 266:14885–14888.

    Google Scholar 

  • Janssen, G. M. C., Van Damme, H. T. F., Kriek, J., Amons, R., and Moller, W. (1994) J. Biol. Chem. 269:31410–31417.

    Google Scholar 

  • Kawaguchi, Y., Bruni, R., and Roizman, B. (1997) J. Virol. 71:1019–1024.

    Google Scholar 

  • Kinzy, T. G. and Woolford, Jr, J. R. (1995) Genetics 141:481–489.

    Google Scholar 

  • Koonin, E. V., Mushegian, A. R., Tatusov, R. L., Altschul, S. F., Bryant, S. H., Bork, P., and Valencia, A. (1994) Protein Science 3:2045–2054.

    Google Scholar 

  • Lew, Y., Jones, D. V., Mars, W. M., Evans, D., Byrd, D., and Frazier, M. L. (1992) Pancreas 7:144–152.

    Google Scholar 

  • Matsumoto, S., Terui, Y., Xi, S. X., Taira, H., and Ejiri, S. (1994) Febs Lett. 338:103–106.

    Google Scholar 

  • Merrick, W. C. and Hershey, J. W. B. (1996) in Translational Control (Hershey, J. W. B., Mathews, M. B., and Sonenberg, N., Eds.), CSHL Press, pp. 31–69.

  • Mimori, K., Mori, M., Inoue, H., Mafune, K., Akiyoshi, T., and Sugimachi, K. (1996) Gut 38:66–70.

    Google Scholar 

  • Mimori, K., Mori, M., Tanaka, S., Akiyoshi, T., and Sugimachi, K. (1995) Cancer 75:1446–1449.

    Google Scholar 

  • Minella, O., Cormier, P., Morales, J., Poulhe, R., Bellé, R., and Mulner-Lorillon, O. (1994) Cell. Mol. Biol. 40:521–525.

    Google Scholar 

  • Minella, O., Mulner-Lorillon, O., Poulhe, R., Bellé, R., and Cormier, P. (1996a) Eur. J. Biochem. 237:685–690.

    Google Scholar 

  • Minella, O., Mulner-Lorillon, O., Desmedt, V., Hourdez, S., Cormier, P., and Bellé, R. (1996b) Cell. Mol. Biol. 42:805–810.

    Google Scholar 

  • Moldave, K. (1985) Ann. Rev. Biochem. 54:1109–1149.

    Google Scholar 

  • Morales, J., Cormier, P., Mulner-Lorillon, O., Poulhe, R. and Bellé R. (1992) Nucl. Acids Res. 20:4091.

    Google Scholar 

  • Motorin, Y. A., Wolfson, A. D., Orlovsky, A. F., and Gladilin, K. L. (1988) Febs Lett. 238:262–264.

    Google Scholar 

  • Mulner-Lorillon, O., Cormier, P., Cavadore, J.-C., Morales, J., Poulhe, R., and Bellé, R. (1992) Exp. Cell Res. 202:549–551.

    Google Scholar 

  • Mulner-Lorillon, O., Minella, O., Cormier, P., Capony, J. P., Cavadore, J. C., Morales, J., Poulhe, R., and Bellé, R. (1994) J. Biol. Chem. 269:20201–20207.

    Google Scholar 

  • Mulner-Lorillon, O., Poulhe, R., Cormier, P., Labbe, J.-C., Doree, M., and Bellé, R. (1989) Febs Lett. 251:219–224.

    Google Scholar 

  • Nagata, S., Iwasaki, K., and Kasiro, Y. (1976) J. Biochem. 80:73–77.

    Google Scholar 

  • Nygard, O. and Nilsson, L. (1990) Eur. J. Biochem. 191:1–17.

    Google Scholar 

  • O'Shea, E. K., Klemm, J. D., Kim, P. S., and Alber, T. (1991) Science 254:539–544.

    Google Scholar 

  • Peters, H. I., Chang, Y. W. E., and Traugh, J. A. (1995) Eur. J. Biochem. 234:550–556.

    Google Scholar 

  • Riis, B., Rattan, S. I. S., Clark, B. F. C., and Merrick, W. C. (1990) Trends Biochem. Sci. 15:420–424.

    Google Scholar 

  • Sanders, J., Brandsma, M., Janssen, G. M. C., Dijk, J., and Moller, W. (1996) J. Cell Sci. 109:1113–1117.

    Google Scholar 

  • Thompson, R. C. (1988) Trends Biol. Sci. 13:91–93.

    Google Scholar 

  • Venema, R. C., Peters, H. I., and Traugh, J. A. (1991a) J. Biol. Chem. 266:12574–12580.

    Google Scholar 

  • Venema, R. C., Peters, H. I., and Traugh, J. A., (1991b) J. Biol. Chem. 266:11993–11998.

    Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Biologie Cellulaire de l'Ovocyte. Station Biologique de Roscoff, Centre National de la Recherche Scientique (CNRS UPR 9042), Université Pierre et Marie Curie (UPMC), BP 74, 29682, Roscoff cedex., France

    Odile Minella, Odile Mulner-Lorillon, Patrick Cormier & Robert Bellé

  2. Centre National de la Recherche Scientifique (CNRS UPR 9002), 15 rue René Descartes, 67084, Strasbourg cedex, France

    Guillaume Bec

Authors
  1. Odile Minella
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Odile Mulner-Lorillon
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. Guillaume Bec
    View author publications

    You can also search for this author in PubMed Google Scholar

  4. Patrick Cormier
    View author publications

    You can also search for this author in PubMed Google Scholar

  5. Robert Bellé
    View author publications

    You can also search for this author in PubMed Google Scholar

Rights and permissions

Reprints and permissions

About this article

Cite this article

Minella, O., Mulner-Lorillon, O., Bec, G. et al. Multiple Phosphorylation Sites and Quaternary Organization of Guanine-Nucleotide Exchange Complex of Elongation Factor-1 (EF-1βγδ/ValRS) Control the Various Functions of EF-1α. Biosci Rep 18, 119–127 (1998). https://doi.org/10.1023/A:1020140527930

Download citation

  • Issue Date:

  • DOI: https://doi.org/10.1023/A:1020140527930

Search

Navigation