title: ATP synthase superassemblies in animals and plants: two or more are better.
abstract: ATP synthases are part of the sophisticated cellular metabolic network and therefore multiple interactions have to be considered. As discussed in this review, ATP synthases form various supramolecular structures. These include dimers and homooligomeric species. But also interactions with other proteins, particularly those involved in energy conversion exist. The supramolecular assembly of the ATP synthase affects metabolism, organellar structure, diseases, ageing and vice versa. The most common approaches to isolate supercomplexes from native membranes by use of native electrophoresis or density gradients are introduced. On the one hand, isolated ATP synthase dimers and oligomers are employed for structural studies and elucidation of specific protein-protein interactions. On the other hand, native electrophoresis and other techniques serve as tool to trace changes of the supramolecular organisation depending on metabolic alterations. Upon analysing the structure, dimer-specific subunits can be identified as well as interactions with other proteins, for example, the adenine nucleotide translocator. In the organellar context, ATP synthase dimers and oligomers are involved in the formation of mitochondrial cristae. As a consequence, changes in the amount of such supercomplexes affect mitochondrial structure and function. Alterations in the cellular power plant have a strong impact on energy metabolism and ultimately play a significant role in pathophysiology. In plant systems, dimers of the ATP synthase have been also identified in chloroplasts. Similar to mammals, a correlation between metabolic changes and the amount of the chloroplast ATP synthase dimers exists. Therefore, this review focusses on the interplay between metabolism and supramolecular organisation of ATP synthase in different organisms.
authors.affiliation: Clemens-Schöpf-Institute, Department of Chemistry, Physical Biochemistry, Technische Universität Darmstadt, Germany.
authors.forename: Holger
authors.initials: H
authors.lastname: Seelert
authors.forename: Norbert A
authors.initials: NA
authors.lastname: Dencher
mesh_terms: D025181:ATP Synthetase Complexes / Q000737:chemistry / Q000378:metabolism*; D000818:Animals; D015388:Organelles / Q000201:enzymology; D010944:Plants / Q000201:enzymology*; D011487:Protein Conformation
chemical_list: D025181:ATP Synthetase Complexes