Skip to main content

Thank you for visiting nature.com. You are using a browser version with limited support for CSS. To obtain the best experience, we recommend you use a more up to date browser (or turn off compatibility mode in Internet Explorer). In the meantime, to ensure continued support, we are displaying the site without styles and JavaScript.

  • Research
  • Published:

The Intracellular Domain of the Rabbit Prolactin Receptor is Able to Promote the Secretion of a Passenger Protein via an Unusual Secretory Pathway in Lepidopteran Cells

Bio/Technology volume 13, pages 1101–1104 (1995)Cite this article

Abstract

We have previously shown that the intracellular domain of the rabbit prolactin receptor (rbPRL-R), lacking typical signal sequences, was very efficiently secreted into the culture medium when expressed in the baculovirus-insect cell system. We have sought to take advantage of this characteristic for secreting cytoplasmic or nuclear proteins. We have constructed a series of recombinant viruses expressing a foreign gene product fused to the intracellular domain of rbPRL-R. Two passenger genes were used, one encoding a cytoplasmic protein (cyclin B) and the other a nuclear protein (cyclin A). The intracellular domain of rbPRL-R was able to promote the export of these two chimeric proteins with a very high efficiency. This new system should prove useful for secretion of proteins which do not require the post-trans-lational modifications of the classical secretory pathway to be fully active.

This is a preview of subscription content, access via your institution

Access options

Buy this article

  • Purchase on Springer Link
  • Instant access to full article PDF
Buy now

Prices may be subject to local taxes which are calculated during checkout

Similar content being viewed by others

References

  1. Luckow, V.A. 1991. Cloning and expression of heterologous genes in insect cells with baculovirus vectors, p. 97–152. In: Recombinant DNA Technology and Applications. Prokop, A., Bajpan, R. K. and Ho, C. S. (Eds). McGraw-Hill, Inc., N.Y.

    Google Scholar 

  2. Jarvis, D.L. and Summers, M.D. 1992. p. 265–291. In: Recombinant DNA Vaccines: Rationale and Strategies. Isaacson, R. E. (Ed.). Marcel Dekker, N.Y.

    Google Scholar 

  3. Walter, P. and Lingappa, V.R. 1986. Mechanism of protein translocation across the endoplasmic reticulum membrane. Annu. Rev. Cell Biol. 2: 499–516.

    Article  CAS  Google Scholar 

  4. Tessier, D.C., Thomas, D.Y., Khoury, H.E., Lalberte, F. and Vernet, T. 1991. Enhanced secretion from insect cells of a foreign protein fused to the honeybee melittin peptkle. Gene 98: 177–183.

    Article  CAS  Google Scholar 

  5. Murphy, C.I., McIntire, J.R., Hodgdon, H., Seals, J.R. and Young, E. 1993. Enhanced expression, secretion, and large-scale purification of recombinant HIV-I gpl20 in insect cell using the baculovirus egt and p67 signal peptides. Prot. Exp. Purif. 4: 349–357.

    Article  CAS  Google Scholar 

  6. Jarvis, D.L., Summers, M.D., Garcia, A. and Bohlmeyer, D.A. 1993. Influence of different signal peptides and prosequences on expression and secretion of human tissue plasminogen activator in the baculovirus system. J. Biol. Chem. 268: 16754–16762.

    CAS  PubMed  Google Scholar 

  7. Rubartelli, A., Cozzolino, F., Talio, M. and Sitia, R. 1990. A novel secetory pathway for interleukin-lB, a protein lacking a signal sequence. EMBO J. 9: 1503–1510.

    Article  CAS  Google Scholar 

  8. Miyamoto, M., Naruo, K.-I., Seko, C., Matsumoto, S., Kondo, T. and Kurokawa, T. 1993. Molecular cloning of a novel cytokine cDNA encoding the ninth member of the fibroblast growth factor family, which has a unique secretion property. Mol. Cel. Biol. 13: 4251–4259.

    Article  CAS  Google Scholar 

  9. Holland, I.B., Kenny, B. and Blight, M. 1990. Haemolysin secretion from E. coli. Biochimie 72: 131–141.

    Article  CAS  Google Scholar 

  10. Gierse, J.K., Luckow, V.A., Askonas, L.J., Duffin, K.L., Aykent, S., Bild, G.S., Rodi, C.P., Sullivan, M.P., Bourner, M.J., Kimack, N.M. and Krivi, G.G. 1993. High-level expression and purification of human leukotriene A4 hydroxylase from insect cells infected with a baculovirus vector. Prot. Exp. Purif. 4: 358–366.

    Article  CAS  Google Scholar 

  11. Nishimura, C., Matsuura, Y., Kokai, Y., Akers, T., Carper, D., Morjana, N., Lyons, C. and Flynn, T.G. 1990. Cloning and expression of human aldolase reductase. J. Biol. Chem. 265: 9788–9792.

    CAS  PubMed  Google Scholar 

  12. Cahoreau, C., Petridou, B., Cerutti, M., Djiane, J. and Devauchelle, G. 1992. Expression of the full-length prolactin receptor and its specific domains in baculovirus infected insect cells. Biochimie 74: 1053–1065.

    Article  CAS  Google Scholar 

  13. Cahoreau, C., Gamier, L., Djiane, J., Devauchelle, G. and Cerutti, M. 1994. Evidence for N-glycosylation and ubiquitination of the prolactin receptor expressed in a baculovirus-insect cell system. FEBS Letters 350: 230–234.

    Article  CAS  Google Scholar 

  14. Lorca, T., Fesquet, D., Zindy, F., Le Bouffant, F., Cerutti, M., Brechot, C., Devauchelle, G. and Doree, M. 1991. An okadaic acid-sensitive phosphatase negatively controls the cyclin degradation pathway in amphibian eggs. Mol. Cel. Biol. 11: 171–1175.

    Article  Google Scholar 

  15. Kelly, P.A., Ali, S., Rozakis, M., Goujon, L., Nagano, M., Pellegrini, I., Gould, D., Djiane, J., Edery, M., Fimdori, J. and Postel-Vinay, M.C. 1993. The growth hormon/prolactin receptor family, p. 123 In: Recent Progress in Hormon Research, Vol. 48. Academic Press.

    Chapter  Google Scholar 

  16. Finley, D. and Chau, V. 1991. Ubiquitination. Annu. Rev. Cell Biol. 7: 25–69.

    Article  CAS  Google Scholar 

  17. Hershko, A. and Ciechanover, A.A. 1992. The ubiquitin system for protein degradation. Annu. Rev. Biochem. 61: 761–807.

    Article  CAS  Google Scholar 

  18. Zhaung, Z. and McCauley, R. 1989. Ubiquitin is involved in the in vitro insertion of monoamine oxydase B into mitochondrial outer membranes. J. Biol. Chem. 264: 14594–14597.

    CAS  PubMed  Google Scholar 

  19. Mackman, N.K., Baker, K., Gray, L., Haigh, R., Nicaud, J.M. and Holland, I.B. 1987. Release of a chimeric protein into the medium from Escherichia coli using the C-terminal secretion signal of haemolysin. EMBO J. 6: 2835–2841.

    Article  CAS  Google Scholar 

  20. Koronakis, V., Koronakis, E. and Hughes, C. 1989. Isolation and analysis of the C-terminal signal directing export of Escherichia coli hemolysin protein across both bacterial membranes. EMBO J. 8: 595–605.

    Article  CAS  Google Scholar 

  21. Delepelaire, P. and Wandersman, C. 1991. Characterization, localization and transmembrane organization of the three proteins PrtD, PrtE and PrtF necessary for protease secretion by the Gram-negative bacterium Erwinia chrysanihemi. Mol. Microbiol. 5: 2427–2434.

    Article  CAS  Google Scholar 

  22. Wandersman, C. 1992. Secretion across the bacterial outer membrane. Trends Genet. 8: 317–321.

    Article  CAS  Google Scholar 

  23. Higgins, C.F. 1992. ABC transporters: from microorganisms to man. Annu. Rev. Cell Biol. 8: 67–113.

    Article  CAS  Google Scholar 

  24. Croizier, G., Croizier, L., Quiot, J.M. and Lereclus, D. 1988. Recombination of Autographa californica and Rachiplusia ou nuclear polyhedrosis viruses in Galleria mellonella. J. Gen. Virol. 69: 177–185.

    Article  Google Scholar 

  25. Maniatis, T., Fritsch, E.F. and Sambrook, J. 1982. Molecular Cloning: A Laboratory Manual, p. 545. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.

  26. Feigner, P.L. and Ringold, G.M. 1989. Cationic liposome-mediated transfection. Nature 337: 387–388.

    Article  Google Scholar 

  27. Summers, M.D. and Smith, G.E. 1987. A Manual of Methods for Baculovirus Vectors Insect Cell Culture Procedures, p. 1–56. Texas Agric. Exp. St. Bull., no. 1555.

  28. Laemmli, U.K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680–685.

    Article  CAS  Google Scholar 

Download references

Author information

Author notes

  1. Laurence Garnier

    Present address: Department of Microbiology and Immunology, Pennsylvania State University College of Medicine, The Milton S. Hershey Medical Center, 500 University Drive, P.O. Box 850, Hershey, Pennsylvania, 17033

Authors and Affiliations

  1. Laboratoire de Pathologie Compareée, Institut National de la Recherche Agronomique, Centre National de la Recherche Scientifique URA 1184, 30380, Saint-Christol-les-Alèes, France

    Laurence Garnier, Gérard Devauchelle & Martine Cérutti

  2. Laboratoire de Pathologie Compareée, Institut National de la Recherche Agronomique, Centre National de la Recherche Scientifique URA 1184, Université Montpellier II, 34095, Montpellier, Cedex 6, France

    Claire Cahoreau & Gérard Devauchelle

Authors
  1. Laurence Garnier
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Claire Cahoreau
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. Gérard Devauchelle
    View author publications

    You can also search for this author in PubMed Google Scholar

  4. Martine Cérutti
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding author

Correspondence to Laurence Garnier.

Rights and permissions

Reprints and permissions

About this article

Cite this article

Garnier, L., Cahoreau, C., Devauchelle, G. et al. The Intracellular Domain of the Rabbit Prolactin Receptor is Able to Promote the Secretion of a Passenger Protein via an Unusual Secretory Pathway in Lepidopteran Cells. Nat Biotechnol 13, 1101–1104 (1995). https://doi.org/10.1038/nbt1095-1101

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1038/nbt1095-1101

Search

Advanced search

Quick links

Nature Briefing

Sign up for the Nature Briefing newsletter — what matters in science, free to your inbox daily.

Get the most important science stories of the day, free in your inbox. Sign up for Nature Briefing