In vivo iodination of a misfolded proinsulin reveals co-localized signals for Bip binding and for degradation in the ER.

@article{Schmitz1995InVI,
  title={In vivo iodination of a misfolded proinsulin reveals co-localized signals for Bip binding and for degradation in the ER.},
  author={Anton Schmitz and M Maintz and T Kehle and Volker Herzog},
  journal={The EMBO journal},
  year={1995},
  volume={14 6},
  pages={1091-8}
}
The signal for degradation of proteins in the endoplasmic reticulum (ER) is thought to be the exposure of internal domains which are buried when the protein has adopted its correct conformation and which are also exposed in assembly intermediates. This raises the question of why the intermediates are not degraded. We developed a system based on the peroxidase-catalyzed iodination of tyrosine residues which continuously monitors the exposure of internal domains of proinsulin. In CHO cells this… CONTINUE READING
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