Proteomics

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K-562 GalNAc-T1/2 Bump-and-hole Whole cell lysate proteomics data

ABSTRACT: Engineered GalNAc-T glycosyltransferases were used to incorporate a chemically modified GalNAc analog into the glycoproteins on the cell surface of K-562 cells. The chemical modification included a bioorthogonal alkyne tag that allowed for introduction of a clickable, acid-cleavable biotin-picolyl-azide. Glycoproteins were enriched using Streptavidin, and on-bead digestion yielded a peptide fraction that was analysed by mass spectrometry.

INSTRUMENT(S): Orbitrap Fusion

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Suspension Culture

SUBMITTER: Benjamin Schumann  

LAB HEAD: Benjamin Schumann

PROVIDER: PXD017989 | Pride | 2020-04-22

REPOSITORIES: Pride

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Studying posttranslational modifications classically relies on experimental strategies that oversimplify the complex biosynthetic machineries of living cells. Protein glycosylation contributes to essential biological processes, but correlating glycan structure, underlying protein, and disease-relevant biosynthetic regulation is currently elusive. Here, we engineer living cells to tag glycans with editable chemical functionalities while providing information on biosynthesis, physiological context  ...[more]

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