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- W2010478265 abstract "To maintain protein homeostasis in secretory compartments, eukaryotic cells harbor a quality control system that monitors protein folding and protein complex assembly in the endoplasmic reticulum (ER). Proteins that do not fold properly or integrate into cognate complexes are degraded by ER-associated degradation (ERAD) involving retrotranslocation to the cytoplasm and proteasomal peptide hydrolysis. N-linked glycans are essential in glycoprotein ERAD; the covalent oligosaccharide structure is used as a signal to display the folding status of the host protein. In this study, we define the function of the Htm1 protein as an α1,2-specific exomannosidase that generates the Man7GlcNAc2 oligosaccharide with a terminal α1,6-linked mannosyl residue on degradation substrates. This oligosaccharide signal is decoded by the ER-localized lectin Yos9p that in conjunction with Hrd3p triggers the ubiquitin-proteasome–dependent hydrolysis of these glycoproteins. The Htm1p exomannosidase activity requires processing of the N-glycan by glucosidase I, glucosidase II, and mannosidase I, resulting in a sequential order of specific N-glycan structures that reflect the folding status of the glycoprotein." @default.
- W2010478265 created "2016-06-24" @default.
- W2010478265 creator A5001922195 @default.
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- W2010478265 date "2009-01-05" @default.
- W2010478265 modified "2023-10-12" @default.
- W2010478265 title "Htm1 protein generates the N-glycan signal for glycoprotein degradation in the endoplasmic reticulum" @default.
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- W2010478265 doi "https://doi.org/10.1083/jcb.200809198" @default.
- W2010478265 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2615083" @default.
- W2010478265 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/19124653" @default.
- W2010478265 hasPublicationYear "2009" @default.
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