Core 1 O-N-Acetylgalactosamine (O-GalNAc) glycosylation in the human cell nucleus

CEJAS, RB; GARAY, YC; DE LA FUENTE, S; LARDONE RD; IRAZOQUI FJ

BIOLOGICAL CHEMISTRY

WALTER DE GRUYTER & CO

Lugar: Berlin; Año: 2020 vol. 401 p. 1041 - 1041

1431-6730

lycosylation is a very frequent post-translational modification in proteins, and the initiation of O-GalNAc glycosylation has been recently described on relevant nuclear proteins. Here we evaluated the nuclear incorporation of a second sugar residue in the biosynthesis pathway of O-GalNAc glycans to yield the terminal core 1 glycan (C1G, Galβ3GalNAcαSer/Thr). Using confocal microscopy, enzymatic assay, affinity chromatography and mass spectrometry, we analyzed intact cells, purified nuclei and soluble nucleoplasms to identify the essential factors for C1G biosynthesis in the cell nucleus. The enzyme C1GalT1 responsible for C1G synthesis was detected inside the nucleus, while catalytic activity of C1Gal-transferase was present in nucleoplasm and purified nuclei. In addition, C1G were detected in the nucleus inside of intact cells, and nuclear proteins exposing C1G were also identified. These evidences represent the first demonstration of core 1 O-GalNAc glycosylation of prote