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- W2042447745 endingPage "877" @default.
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- W2042447745 abstract "The endoplasmic reticulum (ER) must target potentially toxic misfolded proteins for retrotranslocation and proteasomal degradation while avoiding destruction of productive folding intermediates. For luminal proteins, this discrimination typically depends not only on the folding status of a polypeptide, but also on its glycosylation state. Two putative sugar binding proteins, Htm1p and Yos9p, are required for degradation of misfolded glycoproteins, but the nature of the glycan degradation signal and how such signals are generated and decoded remains unclear. Here we characterize Yos9p's oligosaccharide-binding specificity and find that it recognizes glycans containing terminal α1,6-linked mannose residues. We also provide evidence in vivo that a terminal α1,6-linked mannose-containing oligosaccharide is required for degradation and that Htm1p acts upstream of Yos9p to mediate the generation of such sugars. This strategy of marking potential substrates by Htm1p and decoding the signal by Yos9p is well suited to provide a proofreading mechanism that enhances substrate specificity." @default.
- W2042447745 created "2016-06-24" @default.
- W2042447745 creator A5010255611 @default.
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- W2042447745 date "2008-12-01" @default.
- W2042447745 modified "2023-10-12" @default.
- W2042447745 title "Defining the Glycan Destruction Signal for Endoplasmic Reticulum-Associated Degradation" @default.
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- W2042447745 doi "https://doi.org/10.1016/j.molcel.2008.11.017" @default.
- W2042447745 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2873636" @default.
- W2042447745 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/19111666" @default.
- W2042447745 hasPublicationYear "2008" @default.
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