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- W4220822383 abstract "Abstract Mitochondrial cristae membranes are the oxidative phosphorylation sites in cells. Crista junctions (CJs) form the highly curved neck regions of cristae and are thought to function as selective entry gates into the cristae space. Little is known about how CJs are generated and maintained. We show that the central coiled-coil domain of the mitochondrial contact and cristae organizing system (MICOS) subunit Mic60 forms an elongated, bow tie-shaped tetrameric assembly. Mic19 promotes Mic60 tetramerization via a conserved interface between the Mic60 mitofilin and Mic19 CHCH domains. Dimerization of mitofilin domains exposes a crescent-shaped membrane-binding site with convex curvature tailored to interact with curved CJ necks. Our study suggests that the Mic60-Mic19 subcomplex transverses CJs as a molecular strut, thereby controlling CJ architecture and function." @default.
- W4220822383 created "2022-04-03" @default.
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- W4220822383 date "2022-03-30" @default.
- W4220822383 modified "2023-09-30" @default.
- W4220822383 title "Structural insights into crista junction formation by the Mic60-Mic19 complex" @default.
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- W4220822383 doi "https://doi.org/10.1101/2022.03.30.486340" @default.
- W4220822383 hasPublicationYear "2022" @default.
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