The coordinated action of the MVB pathway and autophagy ensures cell survival during starvation

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Abstract

The degradation and recycling of cellular components is essential for cell growth and survival. Here we show how selective and non-selective lysosomal protein degradation pathways cooperate to ensure cell survival upon nutrient limitation. A quantitative analysis of starvation-induced proteome remodeling in yeast reveals comprehensive changes already in the first three hours. In this period, many different integral plasma membrane proteins undergo endocytosis and degradation in vacuoles via the multivesicular body (MVB) pathway. Their degradation becomes essential to maintain critical amino acids levels that uphold protein synthesis early during starvation. This promotes cellular adaptation, including the de novo synthesis of vacuolar hydrolases to boost the vacuolar catabolic activity. This order of events primes vacuoles for the efficient degradation of bulk cytoplasm via autophagy. Hence, a catabolic cascade including the coordinated action of the MVB pathway and autophagy is essential to enter quiescence to survive extended periods of nutrient limitation.

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Martin Müller

Division of Cell Biology, Biocenter, Medical University of Innsbruck, Innsbruck, Austria

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The authors declare that no competing interests exist.
Oliver Schmidt

Cell Biology, Biocenter, Medical University of Innsbruck, Innsbruck, Austria

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The authors declare that no competing interests exist.
Mihaela Angelova

Division of Bioinformatics, Biocenter, Medical University of Innsbruck, Innsbruck, Austria

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The authors declare that no competing interests exist.
Klaus Faserl

Division of Clinical Biochemistry, ProteinMicroAnalysis Facility, Biocenter, Medical University of Innsbruck, Innsbruck, Austria

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The authors declare that no competing interests exist.
Sabine Weys

Division of Cell Biology, Biocenter, Medical University of Innsbruck, Innsbruck, Austria

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The authors declare that no competing interests exist.
Leopold Kremser

Division of Clinical Biochemistry, ProteinMicroAnalysis Facility, Biocenter, Medical University of Innsbruck, Innsbruck, Austria

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The authors declare that no competing interests exist.
Thaddäus Pfaffenwimmer

Max F. Perutz Laboratories, University of Vienna, Vienna, Austria

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The authors declare that no competing interests exist.
Thomas Dalik

Department of Chemistry, University of Natural Resources and Applied Biosciences, Vienna, Austria

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The authors declare that no competing interests exist.
Claudine Kraft

Max F. Perutz Laboratories, University of Vienna, Vienna, Austria

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The authors declare that no competing interests exist.
Zlatko Trajanoski

Division of Bioinformatics, Biocenter, Medical University of Innsbruck, Innsbruck, Austria

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The authors declare that no competing interests exist.
Herbert Lindner

Division of Clinical Biochemistry, ProteinMicroAnalysis Facility, Biocenter, Medical University of Innsbruck, Innsbruck, Austria

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The authors declare that no competing interests exist.
David Teis

Division of Cell Biology, Biocenter, Medical University of Innsbruck, Innsbruck, Austria

For correspondence
david.teis@i-med.ac.at

Competing interests
The authors declare that no competing interests exist.

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