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

 Previous Article  |  Next Article 

J Virol. 1985 May; 54(2): 374-382

A single amino acid substitution in a hydrophobic domain causes temperature-sensitive cell-surface transport of a mutant viral glycoprotein.

C J Gallione and J K Rose

ABSTRACT

DNA sequences were determined for three cDNA clones encoding vesicular stomatitis virus glycoproteins from the tsO45 mutant (which encodes a glycoprotein that exhibits temperature-sensitive cell-surface transport), the wild-type parent strain, and a spontaneous revertant of tsO45. The DNA sequence analysis showed that as many as three amino acid changes could be responsible for the transport defect. By recombining the cDNA clones in vitro and expressing the recombinants in COS cells, we were able to trace the critical lesion in tsO45 to a single substitution of a polar amino acid (serine) for a hydrophobic amino acid (phenylalanine) in a hydrophobic domain. We suggest that this nonconservative substitution may block protein transport by causing protein denaturation at the nonpermissive temperature. Comparison of the predicted glycoprotein sequences from two vesicular stomatitis virus strains suggests a possible basis for the differential carbohydrate requirement in transport of the two glycoproteins.

J Virol. 1985 May; 54(2): 374-382




This article has been cited by other articles:

  • Townley, A. K., Feng, Y., Schmidt, K., Carter, D. A., Porter, R., Verkade, P., Stephens, D. J. (2008). Efficient coupling of Sec23-Sec24 to Sec13-Sec31 drives COPII-dependent collagen secretion and is essential for normal craniofacial development. J. Cell Sci. 121: 3025-3034 [Abstract] [Full Text]  
  • Chi, S., Cao, H., Chen, J., McNiven, M. A. (2008). Eps15 Mediates Vesicle Trafficking from the trans-Golgi Network via an Interaction with the Clathrin Adaptor AP-1. Mol. Biol. Cell 19: 3564-3575 [Abstract] [Full Text]  
  • Au, J. S.-Y., Puri, C., Ihrke, G., Kendrick-Jones, J., Buss, F. (2007). Myosin VI is required for sorting of AP-1B-dependent cargo to the basolateral domain in polarized MDCK cells. JCB 177: 103-114 [Abstract] [Full Text]  
  • Nadanaka, S., Okada, T., Yoshida, H., Mori, K. (2007). Role of Disulfide Bridges Formed in the Luminal Domain of ATF6 in Sensing Endoplasmic Reticulum Stress. Mol. Cell. Biol. 27: 1027-1043 [Abstract] [Full Text]  
  • Pecot, M. Y., Malhotra, V. (2006). The Golgi Apparatus Maintains Its Organization Independent of the Endoplasmic Reticulum. Mol. Biol. Cell 17: 5372-5380 [Abstract] [Full Text]  
  • Netherton, C. L., McCrossan, M.-C., Denyer, M., Ponnambalam, S., Armstrong, J., Takamatsu, H.-H., Wileman, T. E. (2006). African Swine Fever Virus Causes Microtubule-Dependent Dispersal of the trans-Golgi Network and Slows Delivery of Membrane Protein to the Plasma Membrane. J. Virol. 80: 11385-11392 [Abstract] [Full Text]  
  • Yamasaki, A., Tani, K., Yamamoto, A., Kitamura, N., Komada, M. (2006). The Ca2+-binding Protein ALG-2 Is Recruited to Endoplasmic Reticulum Exit Sites by Sec31A and Stabilizes the Localization of Sec31A. Mol. Biol. Cell 17: 4876-4887 [Abstract] [Full Text]  
  • Rybakin, V., Gounko, N. V., Spate, K., Honing, S., Majoul, I. V., Duden, R., Noegel, A. A. (2006). Crn7 Interacts with AP-1 and Is Required for the Maintenance of Golgi Morphology and Protein Export from the Golgi. J. Biol. Chem. 281: 31070-31078 [Abstract] [Full Text]  
  • Alfalah, M., Krahn, M. P., Wetzel, G., von Horsten, S., Wolke, C., Hooper, N., Kalinski, T., Krueger, S., Naim, H. Y., Lendeckel, U. (2006). A Mutation in Aminopeptidase N (CD13) Isolated from a Patient Suffering from Leukemia Leads to an Arrest in the Endoplasmic Reticulum. J. Biol. Chem. 281: 11894-11900 [Abstract] [Full Text]  
  • Tashima, Y., Taguchi, R., Murata, C., Ashida, H., Kinoshita, T., Maeda, Y. (2006). PGAP2 Is Essential for Correct Processing and Stable Expression of GPI-anchored Proteins. Mol. Biol. Cell 17: 1410-1420 [Abstract] [Full Text]  
  • Moffat, K., Howell, G., Knox, C., Belsham, G. J., Monaghan, P., Ryan, M. D., Wileman, T. (2005). Effects of Foot-and-Mouth Disease Virus Nonstructural Proteins on the Structure and Function of the Early Secretory Pathway: 2BC but Not 3A Blocks Endoplasmic Reticulum-to-Golgi Transport. J. Virol. 79: 4382-4395 [Abstract] [Full Text]  
  • Shen, Y., Hendershot, L. M. (2005). ERdj3, a Stress-inducible Endoplasmic Reticulum DnaJ Homologue, Serves as a CoFactor for BiP's Interactions with Unfolded Substrates. Mol. Biol. Cell 16: 40-50 [Abstract] [Full Text]  
  • Nadanaka, S., Yoshida, H., Kano, F., Murata, M., Mori, K. (2004). Activation of Mammalian Unfolded Protein Response Is Compatible with the Quality Control System Operating in the Endoplasmic Reticulum. Mol. Biol. Cell 15: 2537-2548 [Abstract] [Full Text]  
  • Kamada, A., Nagaya, H., Tamura, T., Kinjo, M., Jin, H.-Y., Yamashita, T., Jimbow, K., Kanoh, H., Wada, I. (2004). Regulation of Immature Protein Dynamics in the Endoplasmic Reticulum. J. Biol. Chem. 279: 21533-21542 [Abstract] [Full Text]  
  • Soza, A., Norambuena, A., Cancino, J., de la Fuente, E., Henklein, P., Gonzalez, A. (2004). Sorting Competition with Membrane-permeable Peptides in Intact Epithelial Cells Revealed Discrimination of Transmembrane Proteins Not Only at the trans-Golgi Network but Also at Pre-Golgi Stages. J. Biol. Chem. 279: 17376-17383 [Abstract] [Full Text]  
  • Jeetendra, E., Ghosh, K., Odell, D., Li, J., Ghosh, H. P., Whitt, M. A. (2003). The Membrane-Proximal Region of Vesicular Stomatitis Virus Glycoprotein G Ectodomain Is Critical for Fusion and Virus Infectivity. J. Virol. 77: 12807-12818 [Abstract] [Full Text]  
  • Tisdale, E. J., Wang, J., Silver, R. B., Artalejo, C. R. (2003). Atypical Protein Kinase C Plays a Critical Role in Protein Transport from Pre-Golgi Intermediates. J. Biol. Chem. 278: 38015-38021 [Abstract] [Full Text]  
  • Husain, M., Moss, B. (2002). Similarities in the Induction of Post-Golgi Vesicles by the Vaccinia Virus F13L Protein and Phospholipase D. J. Virol. 76: 7777-7789 [Abstract] [Full Text]  
  • Dahm, T., White, J., Grill, S., Füllekrug, J., Stelzer, E. H.K. (2001). Quantitative ER {left-right-arrow} Golgi Transport Kinetics and Protein Separation upon Golgi Exit Revealed by Vesicular Integral Membrane Protein 36 Dynamics in Live Cells. Mol. Biol. Cell 12: 1481-1498 [Abstract] [Full Text]  
  • Lee, T. H., Linstedt, A. D. (2000). Potential Role for Protein Kinases in Regulation of Bidirectional Endoplasmic Reticulum-to-Golgi Transport Revealed by Protein Kinase Inhibitor H89. Mol. Biol. Cell 11: 2577-2590 [Abstract] [Full Text]  
  • de Haan, C. A. M., Vennema, H., Rottier, P. J. M. (2000). Assembly of the Coronavirus Envelope: Homotypic Interactions between the M Proteins. J. Virol. 74: 4967-4978 [Abstract] [Full Text]  
  • Polishchuk, R. S., Polishchuk, E. V., Marra, P., Alberti, S., Buccione, R., Luini, A., Mironov, A. A. (2000). Correlative Light-Electron Microscopy Reveals the Tubular-Saccular Ultrastructure of Carriers Operating between Golgi Apparatus and Plasma Membrane. JCB 148: 45-58 [Abstract] [Full Text]  
  • Rojo, M, Emery, G, Marjomaki, V, McDowall, A., Parton, R., Gruenberg, J (2000). The transmembrane protein p23 contributes to the organization of the Golgi apparatus. J. Cell Sci. 113: 1043-1057 [Abstract]  
  • Garcia-Mata, R., Bebok, Z., Sorscher, E. J., Sztul, E. S. (1999). Characterization and Dynamics of Aggresome Formation by a Cytosolic Gfp-Chimera{image}. JCB 146: 1239-1254 [Abstract] [Full Text]  
  • Tisdale, E. J. (1999). A Rab2 Mutant with Impaired GTPase Activity Stimulates Vesicle Formation from Pre-Golgi Intermediates. Mol. Biol. Cell 10: 1837-1849 [Abstract] [Full Text]  
  • Auerbach, D., Bantle, S., Keller, S., Hinderling, V., Leu, M., Ehler, E., Perriard, J.-C. (1999). Different Domains of the M-Band Protein Myomesin Are Involved in Myosin Binding and M-Band Targeting. Mol. Biol. Cell 10: 1297-1308 [Abstract] [Full Text]  
  • Lee, T. H., Linstedt, A. D. (1999). Osmotically Induced Cell Volume Changes Alter Anterograde and Retrograde Transport, Golgi Structure, and COPI Dissociation. Mol. Biol. Cell 10: 1445-1462 [Abstract] [Full Text]  
  • Cannon, K. S., Helenius, A. (1999). Trimming and Readdition of Glucose to N-Linked Oligosaccharides Determines Calnexin Association of a Substrate Glycoprotein in Living Cells. J. Biol. Chem. 274: 7537-7544 [Abstract] [Full Text]  
  • Lalli, G, Herreros, J, Osborne, S., Montecucco, C, Rossetto, O, Schiavo, G (1999). Functional characterisation of tetanus and botulinum neurotoxins binding domains. J. Cell Sci. 112: 2715-2724 [Abstract]  
  • Chen, W., Feng, Y., Chen, D., Wandinger-Ness, A. (1998). Rab11 Is Required for Trans-Golgi Network-to-Plasma Membrane Transport and a Preferential Target for GDP Dissociation Inhibitor. Mol. Biol. Cell 9: 3241-3257 [Abstract] [Full Text]  
  • Lagging, L. M., Meyer, K., Owens, R. J., Ray, R. (1998). Functional Role of Hepatitis C Virus Chimeric Glycoproteins in the Infectivity of Pseudotyped Virus. J. Virol. 72: 3539-3546 [Abstract] [Full Text]  
  • Cole, N. B., Ellenberg, J., Song, J., DiEuliis, D., Lippincott-Schwartz, J. (1998). Retrograde Transport of Golgi-localized Proteins to the ER. JCB 140: 1-15 [Abstract] [Full Text]  
  • Komiyama, M, Soldati, T, von Arx, P, Perriard, J. (1996). The intracompartmental sorting of myosin alkali light chain isoproteins reflects the sequence of developmental expression as determined by double epitope-tagging competition. J. Cell Sci. 109: 2089-2099 [Abstract]  
  • Hertig, C., Eppenberger-Eberhardt, M, Koch, S, Eppenberger, H. (1996). N-cadherin in adult rat cardiomyocytes in culture. I. Functional role of N-cadherin and impairment of cell-cell contact by a truncated N-cadherin mutant. J. Cell Sci. 109: 1-10 [Abstract]  
  • Durrer, P., Gaudin, Y., Ruigrok, R. W. H., Graf, R., Brunner, J. (1995). Photolabeling Identifies a Putative Fusion Domain in the Envelope Glycoprotein of Rabies and Vesicular Stomatitis Viruses. J. Biol. Chem. 270: 17575-17581 [Abstract] [Full Text]  
  • Pierre, P., Pepperkok, R., Kreis, T. E. (1994). Molecular characterization of two functional domains of CLIP-170 in vivo. J. Cell Sci. 107: 1909-1920 [Abstract]  
  • Tisdale, E. J. (2001). Glyceraldehyde-3-phosphate Dehydrogenase Is Required for Vesicular Transport in the Early Secretory Pathway. J. Biol. Chem. 276: 2480-2486 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»