Transport of vesicular stomatitis virus glycoprotein in a cell-free extract.
نویسندگان
چکیده
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).
منابع مشابه
Transport of the vesicular stomatitis glycoprotein to trans Golgi membranes in a cell-free system.
Terminal steps in the transport of the vesicular stomatitis virus glycoprotein (G protein) in the Golgi stack have been reconstituted in a cell-free system. Incorporation of sialic acid into the oligosaccharide chains of G protein was used to monitor transport into the trans Golgi compartment. Transport-coupled sialylation required cytosol, ATP, an N-ethylmaleimide-sensitive factor extractable ...
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عنوان ژورنال:
- Proceedings of the National Academy of Sciences of the United States of America
دوره 77 7 شماره
صفحات -
تاریخ انتشار 1980