This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Anderson, S J Articles by Sherr, C J Search for Related Content PubMed PubMed Citation Articles by Anderson, S J Articles by Sherr, C J

 Previous Article  |  Next Article 

J Virol. 1984 September; 51(3): 730-741

Subcellular localization of glycoproteins encoded by the viral oncogene v-fms.

ABSTRACT

The McDonough strain of feline sarcoma virus encodes a polyprotein that is cotranslationally glycosylated and proteolytically cleaved to yield transforming glycoproteins specified by the viral oncogene v-fms. The major form of the glycoprotein (gp120fms) contains endoglycosidase H-sensitive, N-linked oligosaccharide chains lacking fucose and sialic acid, characteristic of glycoproteins in the endoplasmic reticulum. Kinetic and steady-state measurements showed that most gp120fms molecules were not converted to mature forms containing complex carbohydrate moieties. Fixed-cell immunofluorescence confirmed that the majority of v-fms-coded antigens were internally sequestered in transformed cells. Dual-antibody fluorescence performed with antibodies to intermediate filaments (IFs) showed that the IFs of transformed cells were rearranged, and their distribution coincided with that of v-fms-coded antigens. No specific disruption of actin cables was observed. The v-fms gene products cofractionated with IFs isolated from virus-transformed cells and reassociated with IFs self-assembled in vitro. A minor population of v-fms-coded molecules (gp140fms) acquired endoglycosidase H-resistant, N-linked oligosaccharide chains containing fucose and sialic acid residues, characteristic of molecules processed in the Golgi complex. Some gp140fms molecules were detected at the plasma membrane and were radiolabeled by lactoperoxidase-catalyzed iodination of live transformed cells. We suggest that v-fms-coded molecules are translated as integral transmembrane glycoproteins, most of which are inhibited in transport through the Golgi complex to the plasma membrane.

This article has been cited by other articles:

• Deng, P., Rettenmier, C. W., Pattengale, P. K. (1996). Structural Requirements for the Ectodomain Cleavage of Human Cell Surface Macrophage Colony-stimulating Factor. J. Biol. Chem. 271: 16338-16343 [Abstract] [Full Text]  
• Quelle, D E, Ashmun, R A, Shurtleff, S A, Kato, J Y, Bar-Sagi, D, Roussel, M F, Sherr, C J (1993). Overexpression of mouse D-type cyclins accelerates G1 phase in rodent fibroblasts.. Genes Dev. 7: 1559-1571 [Abstract]  
• (1993). Direct binding of cyclin D to the retinoblastoma gene product (pRb) and pRb phosphorylation by the cyclin D-dependent kinase CDK4. Genes Dev. 7: 331-342  
• Fuhrmann, U, Vennstrom, B, Beug, H (1989). The mutated, myeloid cell-specific growth factor receptor v-fms transforms avian erythroid but not myeloid cells.. Genes Dev. 3: 2072-2082 [Abstract]  
• Weinberg, R. (1985). The action of oncogenes in the cytoplasm and nucleus. Science 230: 770-776 [Abstract]  
• Rettenmier, C., Chen, J., Roussel, M., Sherr, C. (1985). The product of the c-fms proto-oncogene: a glycoprotein with associated tyrosine kinase activity. Science 228: 320-322 [Abstract]