Effect of alternative glycosylation on insulin receptor processing.

@article{Hwang1999EffectOA,
  title={Effect of alternative glycosylation on insulin receptor processing.},
  author={Joseph K. Hwang and Susan C Frost},
  journal={The Journal of biological chemistry},
  year={1999},
  volume={274 32},
  pages={
          22813-20
        }
}
The mature insulin receptor is a cell surface heterotetrameric glycoprotein composed of two alpha- and two beta-subunits. In 3T3-L1 adipocytes as in other cell types, the receptor is synthesized as a single polypeptide consisting of uncleaved alpha- and beta-subunits, migrating as a 190-kDa glycoprotein. To examine the importance of N-linked glycosylation on insulin receptor processing, we have used glucose deprivation as a tool to alter protein glycosylation. Western blot analysis shows that… CONTINUE READING
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