The ATP synthase protein plays an essential role in bioenergetics as it catalyzes the formation of ATP through the rotatory movement of the membrane-spanning subunit.
The ATP synthase protein plays an essential role in bioenergetics as it catalyzes the formation of ATP through the rotatory movement of the membrane-spanning subunit. In mitochondria, the ATP synthase forms dimers through specific interactions between specific subunits of the protein. The dimeric form provides the ATP synthase with a spontaneous curvature that sustains their arrangement at the rim of the high-curvature edges of mitochondrial membrane (cristae). In this talk, I will explore the rotatory movement of ATP synthase as a complementary mechanism for membrane remodelling and self-assembly. Based on tether pulling experiments, an active curvature sensing of ATP synthase is found. The curvature-seeking behaviour is grounded on the membrane softening produced by a local disruption of the lipid packing at the vicinity of rotating proteins as shown by coarse-grained simulations, leading to enhanced membrane fluctuations and frequent protein-protein contacts. Overall, these results suggest a new role for the protein rotation on the dynamic self-assembly of ATP synthases in biological membranes.
Fecha del seminario: 16/06/2022 12:00
Lugar del seminario: Salón de Actos
Ponente del seminario: Iván López Montero
