Fatty acid synthase is preferentially degraded by autophagy upon nitrogen starvation in yeast

Tomer Shpilka, Evelyn Welter, Noam Borovsky, Nira Amar, Frida Shimron, Yoav Peleg, Zvulun Elazar

Research output: Contribution to journalArticlepeer-review

Abstract

Autophagy, an evolutionarily conserved intracellular catabolic process, leads to the degradation of cytosolic proteins and organelles in the vacuole/lysosome. Different forms of selective autophagy have recently been described. Starvation-induced protein degradation, however, is considered to be nonselective. Here we describe a novel interaction between autophagy-related protein 8 (Atg8) and fatty acid synthase (FAS), a pivotal enzymatic complex responsible for the entire synthesis of C16- and C18-fatty acids in yeast. We show that although FAS possesses housekeeping functions, under starvation conditions it is delivered to the vacuole for degradation by autophagy in a Vac8- and Atg24-dependent manner. We also provide evidence that FAS degradation is essential for survival under nitrogen deprivation. Our results imply that during nitrogen starvation specific proteins are preferentially recruited into autophagosomes.

Original languageEnglish
Pages (from-to)1434-1439
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume112
Issue number5
DOIs
StatePublished - 3 Feb 2015

All Science Journal Classification (ASJC) codes

  • General

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