Mayya, ChaithraChaithraMayyaHema Naveena, A.A.Hema NaveenaSinha, PankhuriPankhuriSinhaBhatia, DhirajDhirajBhatia2025-08-312025-08-312024-03-0110.1007/s12038-024-00432-z2-s2.0-85186236909https://d8.irins.org/handle/IITG2025/2900738445557Multiple endocytic processes operate in cells in tandem to uptake multiple cargoes involved in diverse cellular functions, including cell adhesion and migration. The best-studied clathrin-mediated endocytosis (CME) involves the formation of a well-defined cytoplasmic clathrin coat to facilitate cargo uptake. According to the glycolipid–lectin (GL–Lect) hypothesis, galectin-3 (Gal3) binds to glycosylated membrane receptors and glycosphingolipids (GSLs) to drive membrane bending and tubular membrane invaginations that undergo scission to form a morphologically distinct class of uptake structures, termed clathrin-independent carriers (CLICs). Which components from cytoskeletal machinery are involved in the scission of CLICs remains to be explored. In this study, we propose that dynein is recruited onto Gal3-induced tubular endocytic pits and provides the pulling force for friction-driven scission. The uptake of Gal3 and its cargoes (CD98/CD147) is significantly dependent on dynein activity, whereas only transferrin (CME marker) is slightly affected upon dynein inhibition. Our study reveals that Gal3 and Gal3-dependent (CD98 and CD147) clathrin-independent cargoes require dynein for the clathrin-independent endocytosis.falseCD98/CD147 | clathrin-independent endocytosis | dynein | galectin-3/galectin-8Article09737138March 2024142arJournal1WOS:001171545100001