Litcius/Paper detail

The SH3 domain in the fucosyltransferase FUT8 controls FUT8 activity and localization and is essential for core fucosylation

Seita Tomida, Misaki Takata, Tetsuya Hirata, Masamichi Nagae, Miyako Nakano, Yasuhiko Kizuka

2020Journal of Biological Chemistry35 citationsDOIOpen Access PDF

Abstract

and identified His-535 in the SH3 domain as the critical residue for enzymatic activity of FUT8. Furthermore, we found that although FUT8 is mainly localized to the Golgi, it also partially localizes to the cell surface in an SH3-dependent manner, indicating that the SH3 domain is also involved in FUT8 trafficking. Finally, we identified ribophorin I (RPN1), a subunit of the oligosaccharyltransferase complex, as an SH3-dependent binding protein of FUT8. RPN1 knockdown decreased both FUT8 activity and core fucose levels, indicating that RPN1 stimulates FUT8 activity. Our findings indicate that the SH3 domain critically controls FUT8 catalytic activity and localization and is required for binding by RPN1, which promotes FUT8 activity and core fucosylation.

Topics & Concepts

FucosylationFucosyltransferaseFucoseSH3 domainGolgi apparatusChemistryBiochemistryCell biologyProto-oncogene tyrosine-protein kinase SrcGlycanSignal transductionBiologyGlycoproteinEndoplasmic reticulumEnzymeGlycosylation and Glycoproteins ResearchGalectins and Cancer BiologyCellular transport and secretion