A receptor with divided loyalties

The epidermal growth factor receptor (EGFR) is caught in a tug-of-war between two membrane domains, as Lajoie et al. reveal. Which domain wins the competition for this division-promoting protein helps determine whether a cell becomes cancerous.

Creating one of the domains is Caveolin1 (Cav1), which congregates in plasma membrane indentations called caveolae. Cav1 clusters pen in EGFR molecules and block them from relaying progrowth signals into the cell. Cav1 is faulty or absent in many tumors. Another domain, the galectin lattice, forms when galectin molecules interlink glycoproteins on the cell surface. The enzyme Mgat5 promotes these connections by modifying the ends of the glycoproteins. The researchers previously showed that the lattice holds EGFR at the membrane and increases cells' sensitivity to growth stimulators such as epidermal growth factor (EGF)....