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Acceptors stability modulates the efficiency of post-translational protein N-glycosylation

FASEB J. 2024-07; 
Paula M Couto, Carlos M A Guardia, Facundo L Couto, Carlos A Labriola, María S Labanda, Julio J Caramelo
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Proteins, Expression, Isolation and Analysis … The gene encoding the “super folder” variant of the green fluorescent protein from Aequorea victoria (sfGFP) was synthesized (GenScript Piscataway, NJ, USA) and cloned into a … Get A Quote

摘要

N-glycosylation is the most common protein modification in the eukaryotic secretory pathway. It involves the attachment a high mannose glycan to Asn residues in the context of Asn-X-Ser/Thr/Cys, a motif known as N-glycosylation sequon. This process is mediated by STT3A and STT3B, the catalytic subunits of the oligosaccharyltransferase complexes. STT3A forms part of complexes associated with the SEC61 translocon and functions co-translationally. Vacant sequons have another opportunity for glycosylation by complexes carrying STT3B. Local sequence information plays an important role in determining N-glycosylation efficiency, but non-local factors can also have a significant impact. For instance, certain proteins a... More

关键词

N‐glycosylation, STT3B, acceptor stability, oligosaccharyltransferase, sequon efficiency