ArticleProceedings of the National Academy of Sciences of the United States of America2016
Cardiolipin binds selectively but transiently to conserved lysine residues in the rotor of metazoan ATP synthases.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 82 papers.
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82 citing papers in PubMed, 137 citations in OpenAlex.
- Cardiolipin dynamics promote membrane remodeling by mitochondrial OPA1.Nature communications · 2025Article
- An integrative modelling approach to the mitochondrial cristae.Communications biology · 2025Article
- The Role of Cardiolipin in Brain Bioenergetics, Neuroinflammation, and Neurodegeneration.Molecular neurobiology · 2025Review
- Epstein-Barr virus-driven cardiolipin synthesis sustains metabolic remodeling during B cell transformation.Science advances · 2025Article
- Role of cardiolipin in proton transmembrane flux and localization.Biophysical journal · 2025Article
- Electric Forces and ATP Synthesis.Reviews of physiology, biochemistry and pharmacology · 2025Review
- Review
- Epstein-Barr-Virus-Driven Cardiolipin Synthesis Sustains Metabolic Remodeling During B-cell Lymphomagenesis.Research square · 2024Article
- Review
- Mechanism of proton-powered c-ring rotation in a mitochondrial ATP synthase.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Bile acid fitness determinants of amBio · 2024Article
- Membrane platform protein PulF of themBio · 2024Article
- Cationic Proteins Rich in Lysine Residue Trigger Formation of Non-bilayer Lipid Phases in Model and Biological Membranes: Biophysical Methods of Study.The Journal of membrane biology · 2023Review
- Rotation of the c-Ring Promotes the Curvature Sorting of Monomeric ATP Synthases.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023Article
- Bile acid fitness determinants of abioRxiv : the preprint server for biology · 2023Article
- Directed proton transfer from FBiophysical reviews · 2023Review
- Gasdermins gone wild: new roles for GSDMs in regulating cellular homeostasis.Trends in cell biology · 2023Review
- Membrane Lipid Composition Influences the Hydration of Proton Half-Channels in FLife (Basel, Switzerland) · 2023Article
- HILPDA-mediated lipidomic remodelling promotes radiotherapy resistance in nasopharyngeal carcinoma by accelerating mitophagy.Cellular and molecular life sciences : CMLS · 2023Article
- Activity modulation of theiScience · 2023Article
22 more citing papers are in PubMed but not listed here.
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3 authors at 1 institution in 1 country.
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Abstract
The anionic lipid cardiolipin is an essential component of active ATP synthases. In metazoans, their rotors contain a ring of eight c-subunits consisting of inner and outer circles of N- and C-terminal α-helices, respectively. The beginning of the C-terminal α-helix contains a strictly conserved and fully trimethylated lysine residue in the lipid head-group region of the membrane. Larger rings of known structure, from c9-c15 in eubacteria and chloroplasts, conserve either a lysine or an arginine residue in the equivalent position. In computer simulations of hydrated membranes containing trimethylated or unmethylated bovine c8-rings and bacterial c10- or c11-rings, the head-groups of cardiolipin molecules became associated selectively with these modified and unmodified lysine residues and with adjacent polar amino acids and with a second conserved lysine on the opposite side of the membrane, whereas phosphatidyl lipids were attracted little to these sites. However, the residence times of cardiolipin molecules with the ring were brief and sufficient for the rotor to turn only a fraction of a degree in the active enzyme. With the demethylated c8-ring and with c10- and c11-rings, the density of bound cardiolipin molecules at this site increased, but residence times were not changed greatly. These highly specific but brief interactions with the rotating c-ring are consistent with functional roles for cardiolipin in stabilizing and lubricating the rotor, and, by interacting with the enzyme at the inlet and exit of the transmembrane proton channel, in participation in proton translocation through the membrane domain of the enzyme.
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