Galectin-3 drives glycosphingolipid-dependent biogenesis of clathrin-independent carriers.

Many cell surface receptors are internalized by clathrin-independent endocytosis, but how clathrin-independent carriers (CLICs) are generated at the plasma membrane remained unclear. Johannes and colleagues now report that galectin-3 (Gal3) binds to glycosylated cargo proteins and glycosphingolipids. These interactions induce membrane deformation, revealing a mechanism for CLIC biogenesis.