RT Journal Article
T1 Rotation of the c-Ring Promotes the Curvature Sorting of Monomeric ATP Synthases
A1 Valdivieso González, David
A1 Makowski, Marcin
A1 Lillo, M. Pilar
A1 Cao García, Francisco Javier
A1 Melo, Manuel N.
A1 Almendro Vedia, Víctor Galileo
A1 López Montero, Iván
AB ATP synthases are proteins that catalyse the formation of ATP through the rotatory movement of their membrane-spanning subunit. In mitochondria,ATP synthases are found to arrange as dimers at the high-curved edges of cristae. Here, a direct link is explored between the rotatory movement of ATP synthases and their preference for curved membranes. An active curvature sorting of ATP synthases in lipid nanotubes pulled from giant vesicles is found. Coarse-grained simulations confirm the curvature-seeking behaviour of rotating ATP synthases, promoting reversible and frequent protein-protein contacts. The formation of transient protein dimers relies on the membrane-mediated attractive interaction of the order of 1.5 kBT produced by a hydrophobic mismatch upon protein rotation. Transient dimers are sustained by a conic-like arrangement characterized by a wedge angle of 𝜽 ≈ 50°, producing a dynamic coupling between protein shape and membrane curvature. The results suggest a new role of the rotational movement of ATP synthases for their dynamic self-assembly in biological membranes.
PB Wiley-VCH GmbH
YR 2023
FD 2023-09-13
LK https://hdl.handle.net/20.500.14352/115558
UL https://hdl.handle.net/20.500.14352/115558
LA eng
NO D. Valdivieso González, M. Makowski, M. P. Lillo, F. J. Cao-García, M. N. Melo, V. G. Almendro-Vedia, I. López-Montero, Rotation of the c-Ring Promotes the Curvature Sorting of Monomeric ATP Synthases. Adv. Sci. 2023, 10, 2301606. https://doi.org/10.1002/advs.202301606
NO Ministerio de Ciencia e Innovación
NO Comunidad Autónoma de Madrid
NO Universidad Complutense de Madrid
DS Docta Complutense
RD 9 abr 2025