A shared endoplasmic reticulum-associated degradation pathway involving the EDEM1 protein for glycosylated and nonglycosylated proteins.

@article{Shenkman2013ASE,
  title={A shared endoplasmic reticulum-associated degradation pathway involving the EDEM1 protein for glycosylated and nonglycosylated proteins.},
  author={Marina Shenkman and Bella Groisman and Efrat Ron and Edward Avezov and Linda M Hendershot and Gerardo Zelmar Lederkremer},
  journal={The Journal of biological chemistry},
  year={2013},
  volume={288 4},
  pages={
          2167-78
        }
}
Studies of misfolded protein targeting to endoplasmic reticulum-associated degradation (ERAD) have largely focused on glycoproteins, which include the bulk of the secretory proteins. Mechanisms of targeting of nonglycosylated proteins are less clear. Here, we studied three nonglycosylated proteins and analyzed their use of known glycoprotein quality control and ERAD components. Similar to an established glycosylated ERAD substrate, the uncleaved precursor of asialoglycoprotein receptor H2a, its… CONTINUE READING

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