Listeria monocytogenes cell invasion: a new role for cofilin in co-ordinating actin dynamics and membrane lipids.

Actin reorganization, mediated by the actin dynamizing protein cofilin, is essential for host cell invasion by the intracellular pathogenic bacterium Listeria monocytogenes. During invasion, the InlB bacterial surface ligands closely interact with host cell Met receptors to induce phagocytosis. In this issue of Molecular Microbiology, Han et al., 2011 clearly demonstrate that phospholipase D (PLD)-dependent production of membrane phosphatidic acid is required for invasion. They further show that the phosphorylated form of cofilin, which is inactive in actin binding, is necessary for the activation of the PLD1 isoform. Although cofilin-independent PLD2 can also mediate internalization, it is a phospho-cofilin-dependent balanced production of phosphatidic acid that is required for optimal Listeria internalization. Cofilin-dependent membrane lipid remodelling has important implications for cofilin function that go well beyond its direct effects on actin.