Oligomerization is essential for transport of vesicular stomatitis viral glycoprotein to the cell surface.
Using ts045, a temperature sensitive strain of Vesicular stomatitis virus, we show that oligomerization of G protein is a prerequisite for its transport from RER to the Golgi apparatus and for its subsequent maturation. While wild-type G forms an oligomer in the RER, ts045 G synthesized at the nonpermissive temperature does not. When the permissive temperature is reinstated, ts045 G forms an oligomer and moves to the Golgi. The state of oligomerization was determined by chemical cross-linking and by the ability of a microinjected monoclonal antibody specific for the carboxy-terminal five amino acids of the cytoplasmic tail of G to cause patching of G in intracellular membranes. We conclude that formation of an oligomer of G protein, probably a trimer, is necessary for G protein maturation.
D001692:Biological Transport; D002451:Cell Compartmentation; D003432:Cross-Linking Reagents; D003593:Cytoplasm / Q000502:physiology; D004220:Disulfides; D004721:Endoplasmic Reticulum / Q000378:metabolism; D006056:Golgi Apparatus / Q000378:metabolism; D007425:Intracellular Membranes / Q000378:metabolism; D046911:Macromolecular Substances; D008562:Membrane Glycoproteins; D008565:Membrane Proteins / Q000378:metabolism*; D009154:Mutation; D011487:Protein Conformation; D011499:Protein Processing, Post-Translational; D013329:Structure-Activity Relationship; D014721:Vesicular stomatitis Indiana virus; D014759:Viral Envelope Proteins; D014764:Viral Proteins / Q000235:genetics / Q000276:immunology / Q000378:metabolism*
D003432:Cross-Linking Reagents; D004220:Disulfides; C028391:G protein, vesicular stomatitis virus; D046911:Macromolecular Substances; D008562:Membrane Glycoproteins; D008565:Membrane Proteins; D014759:Viral Envelope Proteins; D014764:Viral Proteins