Myosin Va (MyoVa) is a protein that functions as a dimer for processive walking on actin filaments. Autoinhibition of MyoVa involves the motor domain (MD) and the globular tail domain (GTD), with the motor adopting a closed, autoinhibited state that is inactive for ATPase activity. This state prevents the unnecessary consumption of ATP and uncontrolled movement when not transporting cargo. MyoVa exists in several states, including closed, half-closed, transition, and open states. The closed state of MyoVa can be changed to a half-closed state when the d-strand temporarily dissociates from the GTD, resulting in the dynamic confirmation of the short side in the triangular-shaped structure, which is called the closed state. In the presence of both a GTBM-containing protein and Rab11a, the half-closed conformation undergoes a significant motion of both the MD and the lever arm (LA), resulting in the disassembly of the hinge structure, which is referred to as a transition state. Finally, the unstable transition conformation quickly shifts to the open conformation, allowing the GTPs to tightly associate with cargo and the MDs to hydrolyze ATP for the walking process. Notably, a single cargo binding of either a GTBM-binding protein or Rab11a is insufficient to effectively activate MyoVa.