Site-specific Analysis of N-glycans of Receptor Tyrosine Kinases

Abstract

Receptor tyrosine kinases are important targets for drug development, and elucidating the mechanisms responsible for their functional regulation is important. Because most receptor tyrosine kinases are regulated by glycans, they are intimately involved in cellular signaling. Based on the site-specific analysis of N-glycans of the ErbB family, the fibroblast growth factor receptor (FGFR) family, and the hepatocyte growth factor receptor (MET), the role of N-glycosylation of each receptor is now being revealed. Site-specific N-glycan occupancy and N-glycan structure are, to some extent, common to different cell types. Given this, it is assumed that there is a mechanism that is responsible for the status of site-specific N-glycosylation. Further site-specific analyses of N-glycans that are associated with receptors promises to be useful for the elucidation of not only the mechanisms responsible for regulation of cell signaling by glycans, but also the mechanisms associated with glycan biosynthesis in general.