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Significance Specialized sugar polymers (oligosaccharides) are necessary for life at the protein, organelle, cell, and organism levels. Processes for degrading oligosaccharides enhance their repertoire of functions, but a potential problem is short circuiting between degradation and synthesis. With the endoplasmic reticulum of mammalian cells, we show how lipid-linked oligosaccharides (LLOs) meant for attachment to proteins are segregated from an immunogenic process that involves their degradation to free oligosaccharides. Specifically, the STT3A isoform of oligosaccharyltransferase only transfers oligosaccharides, while the STT3B isoform can hydrolyze LLOs when not preoccupied with attachment of oligosaccharides to protein. This allows cells to perform both important processes in concert, without problems due to competition.

Mammalian STT3A/B oligosaccharyltransferases segregate N-glycosylation at the translocon from lipid-linked oligosaccharide hydrolysis