Co-localization of galectin-1 with GM1 ganglioside in the course of its clathrin- and raft-dependent endocytosis

• Published in: Cellular and molecular life sciences : CMLS 2008-08, Vol.65 (16), p.2586-2593
• Main Authors: Fajka-Boja, R, Blaskó, A, Kovács-Sólyom, F, Szebeni, G. J, Tóth, G. K, Monostori, É
• Format: Article
• Language: English
• Subjects: Animals; Antigens, CD7 - metabolism; Biochemistry; Biomedical and Life Sciences; Biomedicine; Biophysics; Cell adhesion & migration; Cell Biology; Cell Line; Clathrin - metabolism; clathrin-dependent; Endocytosis; G(M1) Ganglioside - metabolism; Galectin 1 - metabolism; Galectin-1; Glycoproteins; Glycosylation; GM1 ganglioside; Golgi Apparatus - metabolism; Humans; Life Sciences; Ligands; Membrane Microdomains - metabolism; Protein Transport; Proteins; raft-dependent; Rats; Research Article; Temperature; Thermodynamics; Time Factors
• ISSN: 1420-682X; 1420-9071
• DOI: 10.1007/s00018-008-8143-x

Mammalian galectin-1 (Gal-1), a β-galactoside-binding lectin has a prominent role in regulating cell adhesion, cell growth and immune responses. Downregulation of these biological functions may occur via internalization of Gal-1. In the present study we have investigated the mechanism and possible mediator(s) of Gal-1 endocytosis. We show that internalization occurs at a temperature higher than 22 °C in an energy dependent fashion. After one hour incubation Gal-1 localizes in the Golgi system within the cells, and then disappears without accumulation in degradation compartments, such as lysosomes. Based on their strong intracellular co-localization, two glycoconjugates, GM1 ganglioside and CD7 are implicated in the sorting of internalized Gal-1 into Golgi. Other known Gal-1 binding glycoproteins on T cells (CD2, CD3, CD43 and CD45) do not cointernalize with the lectin. Internalization of Gal-1 depends on its lectin activity and follows dual pathways involving clathrin-coated vesicles and raft-dependent endocytosis.