Transport of vesicular stomatitis virus glycoprotein in a cell-free extract.
We describe a cell-free system in which the membrane glycoprotein of vesicular stomatitis virus is rapidly and efficiently transported to membranes of the Golgi complex by a process resembling intracellular protein transport. Transport in vitro is energy-dependent and is accompanied by terminal glycosylation of the membrane glycoprotein (dependent upon UDP-GlcNAc and resulting in resistance to endo-beta-N-acetylglucosaminidase H).
D000818:Animals; D001693:Biological Transport, Active; D002460:Cell Line; D002474:Cell-Free System; D006224:Cricetinae; D005260:Female; D006023:Glycoproteins / Q000378:metabolism*; D006056:Golgi Apparatus / Q000378:metabolism; D008565:Membrane Proteins / Q000378:metabolism*; D009844:Oligosaccharides / Q000378:metabolism; D010053:Ovary; D014721:Vesicular stomatitis Indiana virus / Q000378:metabolism*; D014764:Viral Proteins / Q000378:metabolism*
D006023:Glycoproteins; D008565:Membrane Proteins; D009844:Oligosaccharides; D014764:Viral Proteins