Effects of Altered Cytoplasmic Domains on Transport of the Vesicular Stomatitis Virus Glycoprotein Are Transferable to Other Proteins

LITERATURE CITED

• Doms, R. W., D. S. Keller, A. Helenius, and W. E. Balch. 1987. Role for adenosine triphosphate in regulating the assembly and transport of vesicular stomatitis virus G protein trimers. J. Cell Biol. 105:1957–1969.
   PubMed Web of Science ®Google Scholar
• Doyle, C., M. G. Roth, J. Sambrook, and M.-J. Gething. 1985. Mutations in the cytoplasmic domain of the influenza virus hemagglutinin affect different stages of intracellular transport. J. Cell Biol. 100:704–714.
   PubMedGoogle Scholar
• Doyle, C., J. Sambrook, and M.-J. Gething. 1986. Analysis of progressive deletions of the transmembrane and cytoplasmic domains of influenza hemagglutinin. J. Cell Biol. 103:1193–1204.
   PubMedGoogle Scholar
• Fitting, T., and D. Kabat. 1982. Evidence for a glycoprotein "signal" involved in transport between subcellular organelles: two membrane glycoproteins encoded by murine leukemia virus reach the cell surface at different rates. J. Biol. Chem. 257:14011–14017.
   PubMedGoogle Scholar
• Fukuda, M., J.-L. Guan, and J. K. Rose. 1988. A membrane-anchored form but not the secretory form of human chorionic gonadotropin-α chain acquires polylactosaminoglycan. J. Biol. Chem. 263:5314–5318.
   PubMedGoogle Scholar
• Gething, M.-J., K. McCammon, and J. Sambrook. 1986. Expression of wild-type and mutant forms of influenza hemagglutinin: the role of folding in intracellular transport. Cell 46:939–950.
   PubMedGoogle Scholar
• Guan, J.-L., H. Cao, and J. K. Rose. 1988. Cell-surface expression of a membrane anchored form of the human chorionic gonadotropin α-subunit. J. Biol. Chem. 263:5306–5313.
   PubMedGoogle Scholar
• Guan, J.-L., C. E. Machamer, and J. K. Rose. 1985. Glycosylation allows cell-surface transport of an anchored secretory protein. Cell 42:489–496.
   PubMedGoogle Scholar
• Guillemin, R., P. Brazeau, P. Bohlen, F. Esch, N. Ling, and W. B. Wehrenberg. 1982. Growth hormone-releasing factor from a human pancreatic tumor that caused acromegaly. Science 218:585–587.
   PubMed Web of Science ®Google Scholar
• Kalderon, D., B. L. Roberts, W. D. Richardson, and A. E. Smith. 1984. A short amino acid sequence able to specify nuclear location. Cell 39:499–509.
   PubMed Web of Science ®Google Scholar
• Katz, F. N., J. E. Rothman, V. R. Lingappa, G. Blobel, and H. F. Lodish. 1977. Membrane assembly in vitro: synthesis, glycosylation and asymmetric insertion of a transmembrane glycoprotein. Proc. Natl. Acad. Sci. USA 74:3278–3282.
   PubMed Web of Science ®Google Scholar
• Kreis, T. E., and H. F. Lodish. 1986. Oligomerization is essential for transport of vesicular stomatitis viral glycoprotein to the cell surface. Cell 46:929–937.
   PubMedGoogle Scholar
• Lehrman, M., J. L. Goldstein, M. S. Brown, D. W. Russell, and W. J. Schneider. 1985. Internalization defective LDL receptors produced by genes with nonsense and frameshift mutations that truncate the cytoplasmic domain. Cell 41:735–743.
   PubMed Web of Science ®Google Scholar
• Lodish, H. F., N. Kong, M. Snider, and G. J. A. M. Strous. 1983. Hepatoma secretory proteins migrate from rough endoplasmic reticulum to Golgi at characteristic rates. Nature (London) 304:80–83.
   PubMed Web of Science ®Google Scholar
• Lodish, H. F., N. Kong, S. Hirani, and J. Rasmussen. 1987. A vesicular intermediate in the transport of hepatoma secretory proteins from the rough endoplasmic reticulum to the Golgi complex. J. Cell Biol. 104:221–230.
   PubMedGoogle Scholar
• McEwen, C. R. 1967. Tables for estimating sedimentation through linear concentration gradients of sucrose solution. Anal. Biochem. 20:114–149.
   PubMed Web of Science ®Google Scholar
• Munro, S., and H. R. B. Pelham. 1987. A C-terminal signal prevents secretion of luminal ER proteins. Cell 48:899–907.
   PubMed Web of Science ®Google Scholar
• Paabo, S., B. M. Bhat, W. S. M. Wold, and P. A. Peterson. 1987. A short sequence in the COOH-terminus makes an adenovirus membrane glycoprotein a resident of the endoplasmic reticulum. Cell 50:311–317.
   PubMedGoogle Scholar
• Pierce, J. G., and T. F. Parsons. 1981. Glycoprotein hormones: structure and function. Annu. Rev. Biochem. 50:465–495.
   PubMed Web of Science ®Google Scholar
• Puddington, L., C. E. Machamer, and J. K. Rose. 1986. Cytoplasmic domains of cellular and viral integral membrane proteins substitute for the cytoplasmic domain of the vesicular stomatitis virus glycoprotein in transport to the plasma membrane. J. Cell Biol. 102:2147–2157.
   PubMedGoogle Scholar
• Rose, J. K., W. J. Welch, B. M. Sefton, F. S. Esch, and N. L. Ling. 1980. The vesicular stomatitis virus glycoprotein is anchored in the viral membrane by a hydrophobic domain near theCOOH-terminus. Proc. Natl. Acad. Sci. USA 77:3884–3888.
   PubMed Web of Science ®Google Scholar
• Rose, J. K., and J. E. Bergmann. 1983. Altered cytoplasmic domains affect intracellular transport of the vesicular stomatitis virus glycoprotein. Cell 34:513–524.
   PubMed Web of Science ®Google Scholar
• Shida, H. 1986. Variants of vaccinia virus hemagglutinin altered in intracellular transport. Mol. Cell. Biol. 6:3734–3745.
   PubMedGoogle Scholar
• Sinha, Y. N., F. W. Selby, U. J. Lewis, and W. P. Vanderlaan. 1972. Effects of administering antisera to mouse growth hormone and prolactin on gain in weight and on mammary nucleic acid content of lactating C3H mice. J. Endocrinol. 55:31–40.
   PubMedGoogle Scholar
• Wieland, F. T., M. L. Gleason, T. A. Serafini, and J. E. Rothman. 1987. The rate of flow from the endoplasmic reticulum to the cell surface. Cell 50:289–300.
   PubMed Web of Science ®Google Scholar
• Wills, J. W., R. V. Srinivas, and E. Hunter. 1984. Mutations of the Rous sarcoma virus env gene that affect the transport and subcellular location of the glycoprotein products. J. Cell Biol. 99:2011–2023.
   PubMedGoogle Scholar
• Zuniga, M. C., and L. E. Hood. 1986. Clonal variation in cell surface display of an H-2 protein lacking a cytoplasmic tail. J. Cell Biol. 102:1–10.
   PubMed Web of Science ®Google Scholar