Skip to main content
The Journal of Cell Biology logoLink to The Journal of Cell Biology
. 1988 Jul 1;107(1):79–87. doi: 10.1083/jcb.107.1.79

Recycling glycoproteins do not return to the cis-Golgi

PMCID: PMC2115183  PMID: 2839522

Abstract

Recycling of a number of glycoproteins along the site of action of mannosidase I (the distal endoplasmic reticulum/cis-Golgi) was followed in several different cell lines. Treatment of cells with 1- deoxymannojirimycin (dMM) produced high mannose oligosaccharides at positions otherwise occupied by complex-type oligosaccharides in these glycoproteins. Conversion of high-mannose-type oligosaccharides to complex oligosaccharides of proteins initially synthesized in the presence of dMM was used as a marker for recycling of glycoproteins along the site of action of dMM. In contrast to findings reported by Snider and Rogers (Snider, M. D., and O. C. Rogers. 1986. J. Cell Biol. 103:265-275), removal of dMM did not result in reconversion of high- mannose oligosaccharides to complex-type sugars, even after prolonged periods of culture. We conclude that surface glycoproteins do not recycle through the cis-medial Golgi elements.

Full Text

The Full Text of this article is available as a PDF (1.7 MB).

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Bischoff J., Kornfeld R. The effect of 1-deoxymannojirimycin on rat liver alpha-mannosidases. Biochem Biophys Res Commun. 1984 Nov 30;125(1):324–331. doi: 10.1016/s0006-291x(84)80371-x. [DOI] [PubMed] [Google Scholar]
  2. Dobberstein B., Garoff H., Warren G., Robinson P. J. Cell-free synthesis and membrane insertion of mouse H-2Dd histocompatibility antigen and beta 2-microglobulin. Cell. 1979 Aug;17(4):759–769. doi: 10.1016/0092-8674(79)90316-7. [DOI] [PubMed] [Google Scholar]
  3. Forsee W. T., Schutzbach J. S. Purification and characterization of a phospholipid-dependent alpha-mannosidase from rabbit liver. J Biol Chem. 1981 Jul 10;256(13):6577–6582. [PubMed] [Google Scholar]
  4. Fuhrmann U., Bause E., Legler G., Ploegh H. Novel mannosidase inhibitor blocking conversion of high mannose to complex oligosaccharides. Nature. 1984 Feb 23;307(5953):755–758. doi: 10.1038/307755a0. [DOI] [PubMed] [Google Scholar]
  5. Fuhrmann U., Bause E., Ploegh H. Inhibitors of oligosaccharide processing. Biochim Biophys Acta. 1985 Jun 24;825(2):95–110. doi: 10.1016/0167-4781(85)90095-8. [DOI] [PubMed] [Google Scholar]
  6. Goldstein J. L., Brown M. S., Anderson R. G., Russell D. W., Schneider W. J. Receptor-mediated endocytosis: concepts emerging from the LDL receptor system. Annu Rev Cell Biol. 1985;1:1–39. doi: 10.1146/annurev.cb.01.110185.000245. [DOI] [PubMed] [Google Scholar]
  7. HUNTER W. M., GREENWOOD F. C. Preparation of iodine-131 labelled human growth hormone of high specific activity. Nature. 1962 May 5;194:495–496. doi: 10.1038/194495a0. [DOI] [PubMed] [Google Scholar]
  8. Klausner R. D., Van Renswoude J., Ashwell G., Kempf C., Schechter A. N., Dean A., Bridges K. R. Receptor-mediated endocytosis of transferrin in K562 cells. J Biol Chem. 1983 Apr 25;258(8):4715–4724. [PubMed] [Google Scholar]
  9. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  10. Neefjes J. J., Breur-Vriesendorp B. S., van Seventer G. A., Iványi P., Ploegh H. L. An improved biochemical method for the analysis of HLA-class I antigens. Definition of new HLA-class I subtypes. Hum Immunol. 1986 Jun;16(2):169–181. doi: 10.1016/0198-8859(86)90046-7. [DOI] [PubMed] [Google Scholar]
  11. Neefjes J. J., Hensen E. J., de Kroon T. I., Ploegh H. L. A biochemical characterization of feline MHC products: unusually high expression of class II antigens on peripheral blood lymphocytes. Immunogenetics. 1986;23(5):341–347. doi: 10.1007/BF00398799. [DOI] [PubMed] [Google Scholar]
  12. Omary M. B., Trowbridge I. S. Biosynthesis of the human transferrin receptor in cultured cells. J Biol Chem. 1981 Dec 25;256(24):12888–12892. [PubMed] [Google Scholar]
  13. Parham P., Alpert B. N., Orr H. T., Strominger J. L. Carbohydrate moiety of HLA antigens. Antigenic properties and amino acid sequences around the site of glycosylation. J Biol Chem. 1977 Nov 10;252(21):7555–7567. [PubMed] [Google Scholar]
  14. Phillips D. R., Morrison M. The arrangement of proteins in the human erythrocyte membrane. Biochem Biophys Res Commun. 1970 Jul 27;40(2):284–289. doi: 10.1016/0006-291x(70)91007-7. [DOI] [PubMed] [Google Scholar]
  15. Schneider C., Sutherland R., Newman R., Greaves M. Structural features of the cell surface receptor for transferrin that is recognized by the monoclonal antibody OKT9. J Biol Chem. 1982 Jul 25;257(14):8516–8522. [PubMed] [Google Scholar]
  16. Shackelford D. A., Strominger J. L. Analysis of the oligosaccharides on the HLA-DR and DC1 B cell antigens. J Immunol. 1983 Jan;130(1):274–282. [PubMed] [Google Scholar]
  17. Snider M. D., Rogers O. C. Intracellular movement of cell surface receptors after endocytosis: resialylation of asialo-transferrin receptor in human erythroleukemia cells. J Cell Biol. 1985 Mar;100(3):826–834. doi: 10.1083/jcb.100.3.826. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Snider M. D., Rogers O. C. Membrane traffic in animal cells: cellular glycoproteins return to the site of Golgi mannosidase I. J Cell Biol. 1986 Jul;103(1):265–275. doi: 10.1083/jcb.103.1.265. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Stahl P., Schwartz A. L. Receptor-mediated endocytosis. J Clin Invest. 1986 Mar;77(3):657–662. doi: 10.1172/JCI112359. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Swiedler S. J., Freed J. H., Tarentino A. L., Plummer T. H., Jr, Hart G. W. Oligosaccharide microheterogeneity of the murine major histocompatibility antigens. Reproducible site-specific patterns of sialylation and branching in asparagine-linked oligosaccharides. J Biol Chem. 1985 Apr 10;260(7):4046–4054. [PubMed] [Google Scholar]
  21. Watts C. Rapid endocytosis of the transferrin receptor in the absence of bound transferrin. J Cell Biol. 1985 Feb;100(2):633–637. doi: 10.1083/jcb.100.2.633. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Wieland F. T., Gleason M. L., Serafini T. A., Rothman J. E. The rate of bulk flow from the endoplasmic reticulum to the cell surface. Cell. 1987 Jul 17;50(2):289–300. doi: 10.1016/0092-8674(87)90224-8. [DOI] [PubMed] [Google Scholar]
  23. Woods J. W., Doriaux M., Farquhar M. G. Transferrin receptors recycle to cis and middle as well as trans Golgi cisternae in Ig-secreting myeloma cells. J Cell Biol. 1986 Jul;103(1):277–286. doi: 10.1083/jcb.103.1.277. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. van Beek W., Tulp A., Bolscher J., Blanken G., Roozendaal K., Egbers M. Transient versus permanent expression of cancer-related glycopeptides on normal versus leukemic myeloid cells coinciding with marrow egress. Blood. 1984 Jan;63(1):170–176. [PubMed] [Google Scholar]
  25. van de Rijn M., Geurts van Kessel A. H., Kroezen V., van Agthoven A. J., Verstijnen K., Terhorst C., Hilgers J. Localization of a gene controlling the expression of the human transferrin receptor to the region q12 leads to qter of chromosome 3. Cytogenet Cell Genet. 1983;36(3):525–531. doi: 10.1159/000131967. [DOI] [PubMed] [Google Scholar]

Articles from The Journal of Cell Biology are provided here courtesy of The Rockefeller University Press

RESOURCES