Endoplasmic reticulum quality control of unassembled iron transporter depends on Rer1p-mediated retrieval from the golgi.

@article{Sato2004EndoplasmicRQ,
  title={Endoplasmic reticulum quality control of unassembled iron transporter depends on Rer1p-mediated retrieval from the golgi.},
  author={Miyuki Sato and Ken Sato and Akihiko Nakano},
  journal={Molecular biology of the cell},
  year={2004},
  volume={15 3},
  pages={
          1417-24
        }
}
Endoplasmic reticulum (ER) quality control is a conserved process by which misfolded or unassembled proteins are selectively retained in the endoplasmic reticulum (ER). Failure in oligomerization of multisubunit membrane proteins is one of the events that triggers ER quality control. The transmembrane domains (TMDs) of unassembled subunits are determinants of ER retention in many cases, although the mechanism of the TMD-mediated sorting of unassembled subunits remains elusive. We studied a… CONTINUE READING

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