In situ architecture of the ER–mitochondria encounter structure

Michael R. Wozny, Andrea Luca, Dustin R. Morado, Andrea Picco, Rasha Khaddaj, Pablo Campomanes, Lazar Ivanović, Patrick C. Hoffmann, Elizabeth A. Miller, Stefano Vanni () and Wanda Kukulski ()
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Michael R. Wozny: MRC Laboratory of Molecular Biology
Andrea Luca: University of Fribourg
Dustin R. Morado: MRC Laboratory of Molecular Biology
Andrea Picco: University of Geneva
Rasha Khaddaj: University of Bern
Pablo Campomanes: University of Fribourg
Lazar Ivanović: University of Bern
Patrick C. Hoffmann: MRC Laboratory of Molecular Biology
Elizabeth A. Miller: MRC Laboratory of Molecular Biology
Stefano Vanni: University of Fribourg
Wanda Kukulski: MRC Laboratory of Molecular Biology

Nature, 2023, vol. 618, issue 7963, 188-192

Abstract: Abstract The endoplasmic reticulum and mitochondria are main hubs of eukaryotic membrane biogenesis that rely on lipid exchange via membrane contact sites1–3, but the underpinning mechanisms remain poorly understood. In yeast, tethering and lipid transfer between the two organelles is mediated by the endoplasmic reticulum–mitochondria encounter structure (ERMES), a four-subunit complex of unresolved stoichiometry and architecture4–6. Here we determined the molecular organization of ERMES within Saccharomyces cerevisiae cells using integrative structural biology by combining quantitative live imaging, cryo-correlative microscopy, subtomogram averaging and molecular modelling. We found that ERMES assembles into approximately 25 discrete bridge-like complexes distributed irregularly across a contact site. Each bridge consists of three synaptotagmin-like mitochondrial lipid binding protein domains oriented in a zig-zag arrangement. Our molecular model of ERMES reveals a pathway for lipids. These findings resolve the in situ supramolecular architecture of a major inter-organelle lipid transfer machinery and provide a basis for the mechanistic understanding of lipid fluxes in eukaryotic cells.

Date: 2023
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DOI: 10.1038/s41586-023-06050-3

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