Cvm1 is a component of multiple vacuolar contact sites required for sphingolipid homeostasis
| Autor: | Daniel D. Bisinski, Inês Gomes Castro, Muriel Mari, Stefan Walter, Florian Fröhlich, Maya Schuldiner, Ayelén González Montoro |
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| Přispěvatelé: | Center for Liver, Digestive and Metabolic Diseases (CLDM) |
| Jazyk: | angličtina |
| Rok vydání: | 2022 |
| Předmět: | |
| Zdroj: | The Journal of Cell Biology, 221(8):e202103048. ROCKEFELLER UNIV PRESS Bisinski, D, Castro, I G, Mari, M C, Walter, S, Frohlich, F, Schuldiner, M & González Montoro, A 2022, ' Cvm1 is a component of multiple vacuolar contact sites required for sphingolipid homeostasis ', Journal of Cell Biology, vol. 221, no. 8, e202103048 . https://doi.org/10.1083/jcb.202103048 |
| ISSN: | 0021-9525 |
| DOI: | 10.1083/jcb.202103048 |
| Popis: | Membrane contact sites are specialized platforms formed between most organelles that enable them to exchange metabolites and influence the dynamics of each other. The yeast vacuole is a degradative organelle equivalent to the lysosome in higher eukaryotes with important roles in ion homeostasis and metabolism. Using a high-content microscopy screen, we identified Ymr160w (Cvm1, for contact of the vacuole membrane 1) as a novel component of three different contact sites of the vacuole: with the nuclear endoplasmic reticulum, the mitochondria, and the peroxisomes. At the vacuole–mitochondria contact site, Cvm1 acts as a tether independently of previously known tethers. We show that changes in Cvm1 levels affect sphingolipid homeostasis, altering the levels of multiple sphingolipid classes and the response of sphingolipid-sensing signaling pathways. Furthermore, the contact sites formed by Cvm1 are induced upon a decrease in sphingolipid levels. Altogether, our work identifies a novel protein that forms multiple contact sites and supports a role of lysosomal contacts in sphingolipid homeostasis. |
| Databáze: | OpenAIRE |
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