Nutrient-responsive O-GlcNAcylation dynamically modulates the secretion of glycan-binding protein galectin 3.

ABSTRACT: Endomembrane glycosylation and cytoplasmic O-GlcNAcylation each play essential roles in nutrient sensing, and characteristic changes in glycan patterns have been described in disease states such as diabetes and cancer. These changes in glycosylation have important functional roles and can drive disease progression. However, little is known about the molecular mechanisms underlying how these signals are integrated and transduced into biological effects. Galectins are proteins that bind glycans and that are secreted by a poorly characterized nonclassical secretory mechanism. Once outside the cell, galectins bind to the terminal galactose residues of cell surface glycans and modulate numerous extracellular functions, such as clathrin-independent endocytosis (CIE). Originating in the cytoplasm

SUBMITTER: Mathew MP 

PROVIDER: S-EPMC8920928 | biostudies-literature | 2022 Mar

REPOSITORIES: biostudies-literature