Skip to main content
Cellular and Molecular Life Sciences: CMLS logoLink to Cellular and Molecular Life Sciences: CMLS
. 2008 Jun 26;65(16):2586–2593. doi: 10.1007/s00018-008-8143-x

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

R Fajka-Boja 1,, A Blaskó 1, F Kovács-Sólyom 1, G J Szebeni 1, G K Tóth 2, É Monostori 1
PMCID: PMC11131775  PMID: 18581052

Abstract.

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.

Keywords. Galectin-1, endocytosis, clathrin-dependent, raft-dependent, GM1 ganglioside

Footnotes

Received 20 March 2008; received after revision 04 June 2008; accepted 05 June 2008


Articles from Cellular and Molecular Life Sciences: CMLS are provided here courtesy of Springer

RESOURCES