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- W2116731154 abstract "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." @default.
- W2116731154 created "2016-06-24" @default.
- W2116731154 creator A5001125354 @default.
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- W2116731154 creator A5069564081 @default.
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- W2116731154 date "2012-06-11" @default.
- W2116731154 modified "2023-10-07" @default.
- W2116731154 title "Aberrant substrate engagement of the ER translocon triggers degradation by the Hrd1 ubiquitin ligase" @default.
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- W2116731154 doi "https://doi.org/10.1083/jcb.201203061" @default.
- W2116731154 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3373407" @default.
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