Phosphatidylethanolamine positively regulates autophagy and longevity
MetadataShow full item record
Altmetrics Handle Statistics
Altmetrics DOI Statistics
Autophagy is a cellular recycling program that retards ageing by efficiently eliminating damaged and potentially harmful organelles and intracellular protein aggregates. Here, we show that the abundance of phosphatidylethanolamine (PE) positively regulates autophagy. Reduction of intracellular PE levels by knocking out either of the two yeast phosphatidylserine decarboxylases (PSD) accelerated chronological ageing-associated production of reactive oxygen species and death. Conversely, the artificial increase of intracellular PE levels, by provision of its precursor ethanolamine or by overexpression of the PE-generating enzyme Psd1, significantly increased autophagic flux, both in yeast and in mammalian cell culture. Importantly administration of ethanolamine was sufficient to extend the lifespan of yeast (Saccharomyces cerevisiae), mammalian cells (U2OS, H4) and flies (Drosophila melanogaster). We thus postulate that the availability of PE may constitute a bottleneck for functional autophagy and that organismal life or healthspan could be positively influenced by the consumption of ethanolamine-rich food.
Rockenfeller , P , Koska , M , Pietrocola , F , Minois , N , Knittelfelder , O , Sica , V , Franz , J , Carmona-Gutierrez , D , Kroemer , G & Madeo , F 2015 , ' Phosphatidylethanolamine positively regulates autophagy and longevity ' , Cell death and differentiation , vol. 22 , no. 3 , pp. 499-508 . https://doi.org/10.1038/cdd.2014.219
Cell death and differentiation
Copyright 2015 the Authors. This work is licensed under a Creative Commons Attribution 3.0 Unported License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/3.0/.
DescriptionThis work was supported by the Austrian Science Fund FWF (grants LIPOTOX, I1000-B20, P23490-B12, and P24381-B20) to FM. The authors acknowledge support from NAWI Graz. OK is a member of the PhD program ‘Molecular Enzymology’, funded by the FWF (project W901-B12). GK is supported by the Ligue contre le Cancer (équipe labelisée); Agence National de la Recherche (ANR); Association pour la recherche sur le cancer (ARC); Cancéropôle Ile-de-France; Institut National du Cancer (INCa); Fondation Bettencourt-Schueller; Fondation de France; Fondation pour la Recherche Médicale (FRM); the European Commission (ArtForce); the European Research Council (ERC); the LabEx Immuno-Oncology; the SIRIC Stratified Oncology Cell DNA Repair and Tumour Immune Elimination (SOCRATE); the SIRIC Cancer Research and Personalized Medicine (CARPEM); and the Paris Alliance of Cancer Research Institutes (PACRI).
Items in the St Andrews Research Repository are protected by copyright, with all rights reserved, unless otherwise indicated.