How rotating ATP synthases can modulate membrane structure

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Almendro Vedia, Víctor G. and Natale, Paolo and Valdivieso González, David and Lillo, M. Pilar and Aragones, Juan L. and López-Montero, Iván (2021) How rotating ATP synthases can modulate membrane structure. Archives of Biochemistry and Biophysics, 708 . p. 108939. ISSN 0003-9861

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Official URL: https://doi.org/10.1016/j.abb.2021.108939



Abstract

F1Fo-ATP synthase (ATP synthase) is a central membrane protein that synthetizes most of the ATP in the cell through a rotational movement driven by a proton gradient across the hosting membrane. In mitochondria, ATP synthases can form dimers through specific interactions between some subunits of the protein. The dimeric form of ATP synthase provides the protein with a spontaneous curvature that sustain their arrangement at the rim of the high-curvature edges of mitochondrial membrane (cristae). Also, a direct interaction with cardiolipin, a lipid present in the inner mitochondrial membrane, induces the dimerization of ATP synthase molecules along cristae. The deletion of those biochemical interactions abolishes the protein dimerization producing an altered mitochondrial function and morphology. Mechanically, membrane bending is one of the key deformation modes by which mitochondrial membranes can be shaped. In particular, bending rigidity and spontaneous curvature are important physical factors for membrane remodelling. Here, we discuss a complementary mechanism whereby the rotatory movement of the ATP synthase might modify the mechanical properties of lipid bilayers and contribute to the formation and regulation of the membrane invaginations.


Item Type:Article
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CRUE-CSIC (Acuerdos Transformativos 2021)

Uncontrolled Keywords:F1Fo ATP synthase, Membrane mechanics, Mitochondria, Cristae, Rotation
Subjects:Sciences > Chemistry
Sciences > Chemistry > Chemistry, Physical and theoretical
ID Code:70117
Deposited On:08 Feb 2022 14:32
Last Modified:22 Feb 2022 09:58

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