Glycolipids anchor laminin

Two decades ago researchers considered the possibility that glycolipids could link laminin and other extracellular matrix proteins to the cell, but once integrins were discovered the focus switched to protein–protein interactions. Now on page 179, Li et al. show that the glycolipid galactosyl-sulfatide (gal-sulfatide) is a crucial anchor for laminin in Schwann cells and is necessary for basement membrane assembly. However, intracellular signaling requires protein receptors, such as integrins and dystroglycan.Laminin was known to interact with sulfated glycolipids, but the significance of the interaction was not known. Li et al. found that laminin aggregated on the surface of Schwann cells in vitro only in the presence of gal-sulfatide. Treatment of the cells with an enzyme that removed the sulfate groups from the surface blocked laminin binding. Fibroblasts do not normally make a basement membrane, but when...