Myosin-X sorts actin filaments into parallel bundles and tunes barbed-end dynamics
Whether a molecular motor can spontaneously organize actin filaments into bundles has remained an open question despite decades of in vitro investigation. Here, we show that the dimeric myosin-X, essential for filopodia initiation and extension in cells, is capable of sorting actin filaments into parallel bundles, gathering barbed ends within 1-2 micrometers. We observe that myosin-X processivity is comparable on single filaments and on bundles induced by myosin-X or fascin. Upon reaching barbed ends, myosin-X slows down the addition or removal of actin subunits, in a myosin density-dependent manner. Furthermore, the funneling of myosin-X towards the remaining filaments at the bundle tip increases motor density and triggers dynamic clustering. Together, we propose that the motor activity of myosin-X is sufficient to initiate filopodia, independently of passive crosslinkers such as fascin or fimbrin.