Apr 16, 2020

On identifying the eukaryotic N-glycosylation scramblase by activity correlation profiling

BioRxiv : the Preprint Server for Biology
A. VerchereAnant K. Menon

Abstract

The canonical pathway of N-linked protein glycosylation in yeast and humans involves transfer of the oligosaccharide moiety from the glycolipid Glc3Man9GlcNAc2-PP-dolichol to select asparagine residues in proteins that have been translocated into the lumen of the endoplasmic reticulum (ER). Synthesis of Glc3Man9GlcNAc2-PP-dolichol occurs in two stages, producing first the key intermediate Man5GlcNAc2-PP-dolichol (M5-DLO) on the cytoplasmic face of the ER, followed by translocation of M5-DLO across the ER membrane where the remaining glycosyltransfer reactions occur to complete the structure. The scramblase protein that mediates the translocation of M5-DLO across the ER membrane has not been identified, but activity assays provide compelling evidence that it is an ER membrane protein with exquisite substrate specificity. Here we report on our progress in identifying the M5-DLO/N-glycosylation scramblase via a mass spectrometry-based 'activity correlation profiling' approach.

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Mentioned in this Paper

Establishment and Maintenance of Localization
Biochemical Pathway
Nuclear Import
Classification
RAC-Alpha Serine/Threonine Kinase
Regulation of Biological Process
Amino Acids, I.V. solution additive
AURKB wt Allele
Protein Phosphorylation
Yeasts

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