Fatty acid synthase is preferentially degraded by autophagy upon nitrogen starvation in yeast
| Autor: | Tomer Shpilka, Yoav Peleg, Noam Borovsky, Zvulun Elazar, Frida Shimron, Evelyn Welter, Nira Amar |
|---|---|
| Rok vydání: | 2015 |
| Předmět: |
Saccharomyces cerevisiae Proteins
Multidisciplinary Nitrogen ATG8 Autophagy Saccharomyces cerevisiae Vacuole Biological Sciences Biology Protein degradation BAG3 Cell biology Fatty acid synthase Cytosol medicine.anatomical_structure Biochemistry Lysosome Proteolysis medicine biology.protein Fatty Acid Synthases |
| Zdroj: | Proceedings of the National Academy of Sciences. 112:1434-1439 |
| ISSN: | 1091-6490 0027-8424 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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