Activated full-length myosin-X moves processively on filopodia with large steps toward diverse two-dimensional directions.

ABSTRACT: Myosin-X, (Myo 10), is an unconventional myosin that transports the specific cargos to filopodial tips, and is associated with the mechanism underlying filopodia formation and extension. To clarify the innate motor characteristic, we studied the single molecule movement of a full-length myosin-X construct with leucine zipper at the C-terminal end of the tail (M10^FullLZ) and the tail-truncated myosin-X without artificial dimerization motif (BAP-M10^1-979HMM). M10^FullLZ localizes at the tip of filopodia like myosin-X full-length (M10^Full). M10^FullLZ moves on actin filaments in the presence of PI(3,4,5)P₃, an activator of myosin-X. Single molecule motility analysis revealed that the step sizes of both M10^FullLZ and BA

SUBMITTER: Sato O 

PROVIDER: S-EPMC5346999 | biostudies-literature | 2017 Mar

REPOSITORIES: biostudies-literature