The plasma membrane of eukaryotic cells is constantly remodelled to adapt to specific cellular functions. The endocytic removal of the plasma membrane is carefully balanced with the reinsertion of intracellular membranes. The small GTPase Arf6 is known to be involved in recycling membranes containing lipid rafts back to the plasma membrane, but, so far, no motor protein involved in this process has been identified. On page , Folma Buss and colleagues now discover that myosin 1c (Myo1c) transports lipid-raft-containing membranes from the perinuclear recycling compartment to the plasma membrane. Depleting cells of Myo1c by using siRNA results in the redistribution of lipid raft markers from the cell surface to intracellular membranes. In addition, Myo1c specifically localises to and stabilises the formation of lipid-raft-enriched membrane tubules that extend from the juxtanuclear recycling compartment towards the plasma membrane. Furthermore, Myo1c is required for cellular functions that depend on lipid raft recycling: cells lacking Myo1c have defects in cell spreading, migration, macropinocytosis and pathogen uptake. This motor protein is, therefore, not only important for regulating dynamic membrane remodelling, but – through its role in lipid raft trafficking – is also crucial for numerous cellular processes.
