N-Glycosylation of Lipocalin 2 Is Not Required for Secretion or Exosome Targeting.

ABSTRACT: Lipocalin 2 (LCN2) is a highly conserved secreted adipokine acting as a serum transport protein for small hydrophobic molecules such as fatty acids and steroids. In addition, LCN2 limits bacterial growth by sequestering iron-containing siderophores and further protects against intestinal inflammation and tumorigenesis associated with alterations in the microbiota. Human LCN2 contains one N-glycosylation site conserved in other species. It was postulated that this post-translational modification could facilitate protein folding, protects from proteolysis, is required for proper trafficking from the Golgi apparatus to the cell surface, and might be relevant for effective secretion. We here show that the homologous nucleoside antibiotic tunicamycin blocks N-linked glycosylation

SUBMITTER: Borkham-Kamphorst E 

PROVIDER: S-EPMC5932398 | biostudies-literature | 2018

REPOSITORIES: biostudies-literature