Sequential in vitro enzymatic N-glycoprotein modification reveals site-specific rates of glycoenzyme processing.

ABSTRACT: N-glycosylation is an essential eukaryotic posttranslational modification that affects various glycoprotein properties, including folding, solubility, protein-protein interactions, and half-life. N-glycans are processed in the secretory pathway to form varied ensembles of structures, and diversity at a single site on a glycoprotein is termed 'microheterogeneity'. To understand the factors that influence glycan microheterogeneity, we hypothesized that local steric and electrostatic factors surrounding each site influence glycan availability for enzymatic modification. We tested this hypothesis via expression of reporter N-linked glycoproteins in N-acetylglucosaminyltransferase MGAT1-null HEK293 cells to produce immature Man₅GlcNAc₂ glycoforms (38 glycan sites total). T

SUBMITTER: Adams TM 

PROVIDER: S-EPMC9530959 | biostudies-literature | 2022 Oct

REPOSITORIES: biostudies-literature