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Phosphoproteomic analysis accross the yeast life cycle reveals homeostatic regulation of fatty acyl chain-length by phosphorylation of the fatty acid synthase complex

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Phosphoproteomic analysis accross the yeast life cycle reveals homeostatic regulation of fatty acyl chain-length by phosphorylation of the fatty acid synthase complex

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dc.contributor.author Moreno Torres, Marta
dc.contributor.author Casanovas, Albert
dc.contributor.author Martínez Montañés, Fernando
dc.contributor.author Topolska, Magdalena
dc.contributor.author Marshall, David L.
dc.contributor.author Sprenger, Richard R.
dc.contributor.author Poad, Berwyck L.J.
dc.contributor.author Blanksby, Stephen J.
dc.contributor.author Hermansson, Martin
dc.contributor.author Jensen, Ole N.
dc.contributor.author Ejsing, Christer S.
dc.date.accessioned 2023-05-19T10:04:30Z
dc.date.available 2023-05-19T10:04:30Z
dc.date.issued 2020
dc.identifier.citation Moreno Torres, Marta Casanovas, Albert Martínez Montañés, Fernando Topolska, Magdalena Marshall, David L. Sprenger, Richard R. Poad, Berwyck L.J. Blanksby, Stephen J. Hermansson, Martin Jensen, Ole N. Ejsing, Christer S. 2020 Phosphoproteomic analysis accross the yeast life cycle reveals homeostatic regulation of fatty acyl chain-length by phosphorylation of the fatty acid synthase complex Cell Reports 32 6 1 25
dc.identifier.uri https://hdl.handle.net/10550/86705
dc.description.abstract The ability to remodel lipid metabolism under changing conditions is pivotal for cellular functionality and homeostasis. Here, we characterize the regulatory landscape of phosphorylation-based signaling events across the life cycle of Saccharomyces cerevisiae and determine its impact on the regulation of lipid metabolism. Our data show that 50 lipid metabolic proteins are differentially phosphorylated as cells transit between different physiological states. To identify functional phosphosites, we devised a strategy where multiple phosphosites are simultaneously mutated into phosphomimetic or phosphodeficient alleles and mutants are phenotyped by in-depth lipidomics flux analysis. This uncovers functional phosphosites in the phosphatidate cytidylyltransferase Cds1, the phosphatidylserine synthase Cho1, and Fas2, the α-subunit of the fatty acid synthase (FAS) complex. Furthermore, we show that the fatty acyl chain length produced by FAS is governed by phosphorylation. Overall, our work demonstrates a vital role for phosphoregulation of lipid metabolism and provides a resource to investigate its molecular underpinnings.
dc.language.iso eng
dc.relation.ispartof Cell Reports, 2020, vol. 32, num. 6, p. 1-25
dc.subject Bioquímica
dc.subject Biologia
dc.title Phosphoproteomic analysis accross the yeast life cycle reveals homeostatic regulation of fatty acyl chain-length by phosphorylation of the fatty acid synthase complex
dc.type journal article
dc.date.updated 2023-05-19T10:04:31Z
dc.identifier.doi 10.1016/j.celrep.2020.108024
dc.identifier.idgrec 158854
dc.rights.accessRights open access

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