Structure of the ceramide-bound SPOTS complex

Jan-Hannes Schäfer, Carolin Körner, Bianca M. Esch, Sergej Limar, Kristian Parey, Stefan Walter, Dovile Januliene (), Arne Moeller () and Florian Fröhlich ()
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Jan-Hannes Schäfer: Osnabrück University Department of Biology/Chemistry Structural Biology section
Carolin Körner: Osnabrück University Department of Biology/Chemistry Bioanalytical Chemistry section
Bianca M. Esch: Osnabrück University Department of Biology/Chemistry Bioanalytical Chemistry section
Sergej Limar: Osnabrück University Department of Biology/Chemistry Bioanalytical Chemistry section
Kristian Parey: Osnabrück University Department of Biology/Chemistry Structural Biology section
Stefan Walter: Osnabrück University Center of Cellular Nanoanalytic Osnabrück (CellNanOs)
Dovile Januliene: Osnabrück University Department of Biology/Chemistry Structural Biology section
Arne Moeller: Osnabrück University Department of Biology/Chemistry Structural Biology section
Florian Fröhlich: Osnabrück University Department of Biology/Chemistry Bioanalytical Chemistry section

Nature Communications, 2023, vol. 14, issue 1, 1-12

Abstract: Abstract Sphingolipids are structural membrane components that also function in cellular stress responses. The serine palmitoyltransferase (SPT) catalyzes the rate-limiting step in sphingolipid biogenesis. Its activity is tightly regulated through multiple binding partners, including Tsc3, Orm proteins, ceramides, and the phosphatidylinositol-4-phosphate (PI4P) phosphatase Sac1. The structural organization and regulatory mechanisms of this complex are not yet understood. Here, we report the high-resolution cryo-EM structures of the yeast SPT in complex with Tsc3 and Orm1 (SPOT) as dimers and monomers and a monomeric complex further carrying Sac1 (SPOTS). In all complexes, the tight interaction of the downstream metabolite ceramide and Orm1 reveals the ceramide-dependent inhibition. Additionally, observation of ceramide and ergosterol binding suggests a co-regulation of sphingolipid biogenesis and sterol metabolism within the SPOTS complex.

Date: 2023
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DOI: 10.1038/s41467-023-41747-z

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