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• W2751799886 endingPage "3638" @default.
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• W2751799886 abstract "In metazoan organisms, the STT3A isoform of the oligosaccharyltransferase is localized adjacent to the protein translocation channel to catalyze co-translational N-linked glycosylation of proteins in the endoplasmic reticulum. The mechanism responsible for the interaction between the STT3A complex and the translocation channel has not been addressed. Using genetically modified human cells that are deficient in DC2 or KCP2 proteins, we show that loss of DC2 causes a defect in co-translational N-glycosylation of proteins that mimics an STT3A−/− phenotype. Biochemical analysis showed that DC2 and KCP2 are responsible for mediating the interaction between the protein translocation channel and the STT3A complex. Importantly, DC2- and KCP2-deficient STT3A complexes are stable and enzymatically active. Deletion mutagenesis revealed that a conserved motif in the C-terminal tail of DC2 is critical for assembly into the STT3A complex, whereas the lumenal loop and the N-terminal cytoplasmic segment are necessary for the functional interaction between the STT3A and Sec61 complexes." @default.
• W2751799886 created "2017-09-15" @default.
• W2751799886 creator A5055076326 @default.
• W2751799886 creator A5075463702 @default.
• W2751799886 creator A5079445950 @default.
• W2751799886 date "2017-08-31" @default.
• W2751799886 modified "2023-10-02" @default.
• W2751799886 title "DC2 and KCP2 mediate the interaction between the oligosaccharyltransferase and the ER translocon" @default.
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• W2751799886 doi "https://doi.org/10.1083/jcb.201702159" @default.
• W2751799886 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5674889" @default.
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• W2751799886 hasPublicationYear "2017" @default.
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