@article{Rubenstein2012-06-11Aberr-21018,
  year={2012},
  doi={10.1083/jcb.201203061},
  title={Aberrant substrate engagement of the ER translocon triggers degradation by the Hrd1 ubiquitin ligase},
  number={6},
  volume={197},
  issn={0021-9525},
  journal={The Journal of Cell Biology},
  pages={761--773},
  author={Rubenstein, Eric M. and Kreft, Stefan G. and Greenblatt, Wesley and Swanson, Robert and Hochstrasser, Mark}
}

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    <dc:contributor>Kreft, Stefan G.</dc:contributor>
    <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2012-12-18T07:35:45Z</dc:date>
    <dcterms:bibliographicCitation>Journal of Cell Biology ; 197 (2012), 6. - S. 761-773</dcterms:bibliographicCitation>
    <dc:contributor>Hochstrasser, Mark</dc:contributor>
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    <dc:contributor>Greenblatt, Wesley</dc:contributor>
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    <dc:language>eng</dc:language>
    <dcterms:issued>2012-06-11</dcterms:issued>
    <dc:contributor>Rubenstein, Eric M.</dc:contributor>
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    <dc:creator>Rubenstein, Eric M.</dc:creator>
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    <dc:creator>Swanson, Robert</dc:creator>
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    <dcterms:abstract xml:lang="eng">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 cytoplasmic degron normally recognized by Doa10, to the Sec62 membrane protein rendered the protein a Hrd1 substrate. Hrd1-dependent degradation occurred when Deg1-Sec62 aberrantly engaged the Sec61 translocon channel and underwent topological rearrangement. Mutations that prevent translocon engagement caused a reversion to Doa10-dependent degradation. Similarly, a variant of apolipoprotein B, a protein known to be cotranslocationally targeted for proteasomal degradation, was also a Hrd1 substrate. Hrd1 therefore likely plays a general role in targeting proteins that persistently associate with and potentially obstruct the translocon.</dcterms:abstract>
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    <dc:creator>Kreft, Stefan G.</dc:creator>
    <dc:creator>Hochstrasser, Mark</dc:creator>
    <dc:contributor>Swanson, Robert</dc:contributor>
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