• DOI:10.1042/BST0120519
• Corpus ID: 34203354

Studies of membrane glycoproteins in the rough endoplasmic reticulum.

@article{Atkinson1984StudiesOM,
  title={Studies of membrane glycoproteins in the rough endoplasmic reticulum.},
  author={Paul H. Atkinson and Alisa K. Kabcenell},
  journal={Biochemical Society transactions},
  year={1984},
  volume={12 3},
  pages={
          519-21
        }
}

• P. H. Atkinson, A. Kabcenell
• Published 1 June 1984
• Biology
• Biochemical Society transactions

Studies on membrane glycoproteins which have the RER as their final destination are comparatively rare; thus it has not been possible to examine the initial stages of protein compartmentalization. The roles of the RER and the Golgi apparatus in membrane protein sorting need to be elucidated. It has been suggested, for example, that RER proteins would be returned to the endoplasmic reticulum while the other species would collect in the trans aspect of the Golgi apparatus before being shuttled to their ultimate sites (Rothman, 1981). Viral model systems for exploring RER membrane proteins have not yet been produced and such information as exists concerns ribophorin, a glycoprotein which is quite difficult to work with because of its low abundance and slow rate of turnover. Analogous to the plasma membrane studies, a RER-maturing virus could serve as a useful probe in the elucidation of the behaviour of membrane proteins. Because many lytic viruses completely shut off host RNA and protein synthesis, the addition of radioactive amino acids or sugars leads to the labelling of only virus-specified molecules, which are present in high abundance in the infected cells. The intracellular dynamics of molecules of interest can then be readily followed. This paper discusses various glycoproteins which are located in the RER and their carbohydrate processing. We also describe a new viral model, rotavirus, for studying the behaviour of membrane proteins.