Journal
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume 522, Issue 1, Pages 254-258Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2019.11.089
Keywords
Autophagy; Proteasome; Atg9; Protein degradation; Stress response
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Funding
- William & Ella Owens Medical Foundation
- Cancer Prevention Institute of Texas [RP170686, RP180769]
- Mays Cancer Center
- National Institute of Health [GM118350]
- National Center for Advancing Translational Science [UL1TR002645]
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Autophagy is a highly conserved biological process essential to protein, cellular and organismal homeostasis. As autophagy plays a critical role in cellular responses to various external and internal stimuli, it is important to understand the mechanism underlying autophagy regulation. Here, we monitor the stability of 17 key autophagy factors in the yeast S. cerevisiae and show that Atg9 and Atg14 are degraded under normal growth conditions. Whereas Atg14 is regulated by both the proteasome and autophagy, Atg9 turnover is normally mediated by the proteasome but impeded upon starvation or rapamycin treatment. Interestingly, distinct segments of Atg9 confer instability, suggesting that multiple pathways are involved in Atg9 degradation. Our results provide the foundation to further elucidate the physiological significance of Atg9 turnover and also the interplay between two major proteolytic systems (i.e., autophagy and the proteasome). (C) 2019 Elsevier Inc. All rights reserved.
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