Shintaroh Kubo

F domain of ATP synthase functions as a rotary molecular motor, coupling proton translocation with the rotation of the c-ring rotor. This process involves proton uptake at the entry half channel, rotor rotation, and proton release to the exit half channel. While the overall coupling mechanism is established, the design principle for efficient rotation remains unclear.

Significance Fo motor is the proton-conducting unit of ATP synthase and a rotary motor driven by proton translocation across the membrane. Previous biochemical and structural studies have established the “half-channel model,” which explains how proton translocation is coupled with rotation. However, it remains unclear what structural features enable the smooth coordination of proton flow and rotation for efficient motion. Here, we conducted hybrid molecular dynamics with Monte Carlo simulations.

Abstract Eukaryotic cilia and flagella are thin structures present on the surface of cells, playing vital roles in signaling and cellular motion. Cilia structures rely on intraflagellar transport (IFT), which involves dynein-2 for retrograde and kinesin-2 for anterograde movements along doublet microtubules. Unlike dynein-1, which works on singlet microtubules within the cytoplasm, dynein-2 specifically works on the doublet microtubules inside the cilia.