Sulfur starvation-induced autophagy in Saccharomyces cerevisiae involves SAM-dependent signaling and transcription activator Met4
Magali Prigent,
Hélène Jean-Jacques,
Delphine Naquin,
Stéphane Chédin,
Marie-Hélène Cuif,
Renaud Legouis and
Laurent Kuras ()
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Magali Prigent: Institute for Integrative Biology of the Cell (I2BC)
Hélène Jean-Jacques: Institute for Integrative Biology of the Cell (I2BC)
Delphine Naquin: Institute for Integrative Biology of the Cell (I2BC)
Stéphane Chédin: Institute for Integrative Biology of the Cell (I2BC)
Marie-Hélène Cuif: Institute for Integrative Biology of the Cell (I2BC)
Renaud Legouis: Institute for Integrative Biology of the Cell (I2BC)
Laurent Kuras: Institute for Integrative Biology of the Cell (I2BC)
Nature Communications, 2024, vol. 15, issue 1, 1-16
Abstract:
Abstract Autophagy is a key lysosomal degradative mechanism allowing a prosurvival response to stresses, especially nutrient starvation. Here we investigate the mechanism of autophagy induction in response to sulfur starvation in Saccharomyces cerevisiae. We found that sulfur deprivation leads to rapid and widespread transcriptional induction of autophagy-related (ATG) genes in ways not seen under nitrogen starvation. This distinctive response depends mainly on the transcription activator of sulfur metabolism Met4. Consistently, Met4 is essential for autophagy under sulfur starvation. Depletion of either cysteine, methionine or SAM induces autophagy flux. However, only SAM depletion can trigger strong transcriptional induction of ATG genes and a fully functional autophagic response. Furthermore, combined inactivation of Met4 and Atg1 causes a dramatic decrease in cell survival under sulfur starvation, highlighting the interplay between sulfur metabolism and autophagy to maintain cell viability. Thus, we describe a pathway of sulfur starvation-induced autophagy depending on Met4 and involving SAM as signaling sulfur metabolite.
Date: 2024
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:15:y:2024:i:1:d:10.1038_s41467-024-51309-6
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DOI: 10.1038/s41467-024-51309-6
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