Cvm1 is a component of multiple vacuolar contact sites required for sphingolipid homeostasis
Autor(en): | Bisinski, Daniel D. Castro, Ines Gomes Mari, Muriel Walter, Stefan Frohlich, Florian Schuldiner, Maya Montoro, Ayelen Gonzalez |
Stichwörter: | Cell Biology; ER-MITOCHONDRIA; GOLGI; INTERFACE; JUNCTIONS; PROTEIN TOPOLOGY; SACCHAROMYCES-CEREVISIAE; STRESS; TETHER; YEAST | Erscheinungsdatum: | 2022 | Herausgeber: | ROCKEFELLER UNIV PRESS | Journal: | JOURNAL OF CELL BIOLOGY | Volumen: | 221 | Ausgabe: | 8 | Zusammenfassung: | 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. |
ISSN: | 0021-9525 | DOI: | 10.1083/jcb.202103048 |
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geprüft am 14.05.2024