Dataset Information

Oligosaccharyltransferase is involved in targeting to ER-associated degradation

ABSTRACT: The majority of secretory proteins undergo N-glycosylation, a process catalyzed by oligosaccharyltransferase (OST), a membrane-bound protein complex that associates with the translocation channels within the endoplasmic reticulum (ER). Proteins failing quality control undergo ER-associated degradation (ERAD) by retrotranslocation to cytosolic proteasomes. Using a misfolded protein bait and SILAC proteomics, we unexpectedly identified several OST subunits among top hits. For further details, Please refer to the publication "Oligosaccharyltransferase is involved in targeting to ER-associated degradation" by Marina Shenkman et al..

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Early Embryonic Cell

SUBMITTER: Roman Körner

LAB HEAD: Gerardo Z. Lederkremer

PROVIDER: PXD067654 | Pride | 2025-10-14

REPOSITORIES: Pride

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			Action	DRS
	20090912_FT_TC_115_SA_009_S01.RAW	Raw
	20090912_FT_TC_115_SA_009_S02.RAW	Raw
	20090912_FT_TC_115_SA_009_S03.RAW	Raw
	20090912_FT_TC_115_SA_009_S04.RAW	Raw
	20090912_FT_TC_115_SA_009_S05.RAW	Raw

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Project description:STT3A and STT3B are the main catalytic subunit of oligosaccharyltransferase (OST-A and OST-B in mammalian cells), which primarily mediate cotranslational and posttranslocational N-linked glycosylation, respectively. To determine the specificity of STT3A and STT3B, we performed proteomics and glycoproteomics analyses to characterize the protein expression and glycosylation in STT3A-knockout (KO), STT3B-KO, and wild-type (WT) HEK293 cells. In total, 3,993 proteins, 4,020 unique N-linked intact glycopeptides (IGPs) and 723 glycosites, representing 401 glycoproteins were identified in KO and WT cells. Deletion of the STT3A gene had a greater impact on the protein expression than deletion of STT3B, especially on glycoproteins. In addition, mannosylated N-glycans from glycoproteins were reduced, while fucosylated N-glycans were increased in STT3A-KO cells. The glycan changes may be caused by the differential expression of glycosyltransferases and the activation of unfolded protein response (UPR) with further analysis of glycan-related enzymes. Interestingly, hyperglycosylated proteins were identified in KO cells. We verified that the hyperglycosylation of ENPL was caused by the ER stress and UPR, which were induced by the deletion of the STT3A. Overall, the specificity of STT3A and STT3B revealed that defects in the OST subunit not only broadly affect N-linked glycosylation of the protein but also affect protein expression.STT3A and STT3B are the main catalytic subunit of oligosaccharyltransferase (OST-A and OST-B in mammalian cells), which primarily mediate cotranslational and posttranslocational N-linked glycosylation, respectively. To determine the specificity of STT3A and STT3B, we performed proteomics and glycoproteomics analyses to characterize the protein expression and glycosylation in STT3A-knockout (KO), STT3B-KO, and wild-type (WT) HEK293 cells. In total, 3,993 proteins, 4,020 unique N-linked intact glycopeptides (IGPs) and 723 glycosites, representing 401 glycoproteins were identified in KO and WT cells. Deletion of the STT3A gene had a greater impact on the protein expression than deletion of STT3B, especially on glycoproteins. In addition, mannosylated N-glycans from glycoproteins were reduced, while fucosylated N-glycans were increased in STT3A-KO cells. The glycan changes may be caused by the differential expression of glycosyltransferases and the activation of unfolded protein response (UPR) with further analysis of glycan-related enzymes. Interestingly, hyperglycosylated proteins were identified in KO cells. We verified that the hyperglycosylation of ENPL was caused by the ER stress and UPR, which were induced by the deletion of the STT3A. Overall, the specificity of STT3A and STT3B revealed that defects in the OST subunit not only broadly affect N-linked glycosylation of the protein but also affect protein expression.

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Oligosaccharyltransferase is involved in targeting to ER-associated degradation

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