Abstract
Sindbis virus-infected baby hamster kidney (BHK) cells were analyzed by thin section fracture-label. Specific immunolabel with antiviral glycoprotein antibodies was used in conjunction with colloidal gold- conjugated protein A. As we previously reported (Torrisi, M. R., and S. Bonatti, 1985, J. Cell Biol., 101:1300-1306), Sindbis transmembrane glycoproteins are present in the inner nuclear membrane as well as in the outer nuclear membrane, endoplasmic reticulum, Golgi stacks and vesicles, and plasma membranes. Viral glycoproteins located on the inner nuclear membrane resemble those present on the outer membrane in terms of amount, distribution, and preferential partition after fracture. We show in this paper that Sindbis glycoproteins after treatment with cycloheximide are removed from the inner nuclear membrane with the same kinetics as their counterparts present on the outer membrane. This finding strongly suggests that newly synthesized transmembrane glycoproteins may freely diffuse to and from the inner nuclear membrane before entering into the intracellular transport pathway to the plasma membrane.
Full Text
The Full Text of this article is available as a PDF (2.0 MB).
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Bergmann J. E., Singer S. J. Immunoelectron microscopic studies of the intracellular transport of the membrane glycoprotein (G) of vesicular stomatitis virus in infected Chinese hamster ovary cells. J Cell Biol. 1983 Dec;97(6):1777–1787. doi: 10.1083/jcb.97.6.1777. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Franke W. W., Scheer U., Krohne G., Jarasch E. D. The nuclear envelope and the architecture of the nuclear periphery. J Cell Biol. 1981 Dec;91(3 Pt 2):39s–50s. doi: 10.1083/jcb.91.3.39s. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Gerace L., Blobel G. Nuclear lamina and the structural organization of the nuclear envelope. Cold Spring Harb Symp Quant Biol. 1982;46(Pt 2):967–978. doi: 10.1101/sqb.1982.046.01.090. [DOI] [PubMed] [Google Scholar]
- Gerace L., Ottaviano Y., Kondor-Koch C. Identification of a major polypeptide of the nuclear pore complex. J Cell Biol. 1982 Dec;95(3):826–837. doi: 10.1083/jcb.95.3.826. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Green J., Griffiths G., Louvard D., Quinn P., Warren G. Passage of viral membrane proteins through the Golgi complex. J Mol Biol. 1981 Nov 15;152(4):663–698. doi: 10.1016/0022-2836(81)90122-4. [DOI] [PubMed] [Google Scholar]
- Jamieson J. D., Palade G. E. Intracellular transport of secretory proteins in the pancreatic exocrine cell. 3. Dissociation of intracellular transport from protein synthesis. J Cell Biol. 1968 Dec;39(3):580–588. doi: 10.1083/jcb.39.3.580. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Pinto da Silva P., Parkison C., Dwyer N. Fracture-label:O cytochemistry of freeze-fracture faces in the erythrocyte membrane. Proc Natl Acad Sci U S A. 1981 Jan;78(1):343–347. doi: 10.1073/pnas.78.1.343. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Pinto da Silva P., Torrisi M. R., Kachar B. Freeze-fracture cytochemistry: localization of wheat-germ agglutinin and concanavalin A binding sites on freeze-fractured pancreatic cells. J Cell Biol. 1981 Nov;91(2 Pt 1):361–372. doi: 10.1083/jcb.91.2.361. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Puddington L., Lively M. O., Lyles D. S. Role of the nuclear envelope in synthesis, processing, and transport of membrane glycoproteins. J Biol Chem. 1985 May 10;260(9):5641–5647. [PubMed] [Google Scholar]
- Schindler M., Holland J. F., Hogan M. Lateral diffusion in nuclear membranes. J Cell Biol. 1985 May;100(5):1408–1414. doi: 10.1083/jcb.100.5.1408. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Slot J. W., Geuze H. J. Sizing of protein A-colloidal gold probes for immunoelectron microscopy. J Cell Biol. 1981 Aug;90(2):533–536. doi: 10.1083/jcb.90.2.533. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Torrisi M. R., Bonatti S. Immunocytochemical study of the partition and distribution of Sindbis virus glycoproteins in freeze-fractured membranes of infected baby hamster kidney cells. J Cell Biol. 1985 Oct;101(4):1300–1306. doi: 10.1083/jcb.101.4.1300. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Torrisi M. R., Pinto da Silva P. Compartmentalization of intracellular membrane glycocomponents is revealed by fracture-label. J Cell Biol. 1984 Jan;98(1):29–34. doi: 10.1083/jcb.98.1.29. [DOI] [PMC free article] [PubMed] [Google Scholar]
- da Silva P. P., Parkison C., Dwyer N. Freeze-fracture cytochemistry: thin sections of cells and tissues after labeling of fractures faces. J Histochem Cytochem. 1981 Aug;29(8):917–928. doi: 10.1177/29.8.7276536. [DOI] [PubMed] [Google Scholar]
- da Silva P. P., Torrisi M. R. Freeze-fracture cytochemistry: partition of glycophorin in freeze-fractured human erythrocyte membranes. J Cell Biol. 1982 May;93(2):463–469. doi: 10.1083/jcb.93.2.463. [DOI] [PMC free article] [PubMed] [Google Scholar]
