Galectins have been shown to have a variety of activities associated with binding to extracellular glycoconjugates present on the cell surfaces and extracellular matrices. However, many galectins are detected inside the cells in locations, such as nucleus and phagosomes, suggestive of intracellular functions. In some cases, their translocation from one cellular compartment to another has been demonstrated. Specific functions consistent with intracellular localization have now been documented for some galectins. Galectin-1 and -3 have been identified as pre-mRNA splicing factors. Galectin-3, -7, and -12 have been shown to regulate apoptosis, being either anti-apoptotic or pro-apoptotic. Galectin-3 and -12 have been shown to regulate the cell cycle. The multifunctionality of these galectins is probably related to their ability to interact with multiple proteins. Indeed, a number of intracellular proteins have been identified to interact with galectins, in a manner that is dependent on protein-protein interactions, rather than lectin-carbohydrate interactions. However, their roles in the observed functions of galectins have not yet been established. Galectins have also been shown to recognize intracellular proteins through binding to their saccharide side chains. Future studies may reveal binding of galectins to glycoconjugates on internalized particles including those associated with intracellular microorganisms.
|Original language||English (US)|
|Number of pages||10|
|Journal||Trends in Glycoscience and Glycotechnology|
|State||Published - Jul 2004|
- Intracellular protein trafficking
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)