Cellular function of galectin-7: a critical role in mitochondrial apoptosis

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Apoptosis is an indispensable part of the development and function of an organism. In this process, cells that are no longer needed or that will be detrimental to an organism or tissue are disposed of in a neat and orderly manner to ensure that the damaged cell is packaged and removed cleanly. Among the proteins that play an important role in apoptosis, we find proteins of the bcl-2 family. Members of this family share several structural features that allow them to bind to other intracellular proteins. Our research program aims at better understanding how Bcl-2 proteins interact with galectins. Galectins are soluble carbohydrate-binding proteins that were first discovered in the electric eel more than 35-40 years ago. Since then, the 15 members of the galectin family have been shown to be involved in a number of physiological processes, including development, wound healing, and regulation of the immune response. Historically, studies on galectins have focused on their extracellular functions, most notably because they are able to bind to a variety of receptors expressed at the cell surface. We and others have shown, however, that galectins have equally important functions inside the cells, most notably by controlling apoptosis. The ability of galectin-3 and galectin-7 to localize at the mitochondria and to bind Bcl-2 suggest that they are part of the Bcl-2 network that controls apoptosis. Our research program aims at understanding how intracellular galectins modulate apoptosis via interaction with members of the Bcl-2 family.