Aberrant substrate engagement of the ER translocon triggers degradation by the Hrd1 ubiquitin ligase

@inproceedings{Rubenstein2012AberrantSE,
  title={Aberrant substrate engagement of the ER translocon triggers degradation by the Hrd1 ubiquitin ligase},
  author={Eric M. Rubenstein and Stefan G. Kreft and Wesley Greenblatt and Robert S. Swanson and Mark Hochstrasser},
  booktitle={The Journal of cell biology},
  year={2012}
}
Little is known about quality control of proteins that aberrantly or persistently engage the endoplasmic reticulum (ER)-localized translocon en route to membrane localization or the secretory pathway. Hrd1 and Doa10, the primary ubiquitin ligases that function in ER-associated degradation (ERAD) in yeast, target distinct subsets of misfolded or otherwise abnormal proteins based primarily on degradation signal (degron) location. We report the surprising observation that fusing Deg1, a… CONTINUE READING
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