Autophagy regulator Atg9 is degraded by the proteasome

Guohui Hu, Lizette Rios, Zhengwei Yan, Angela M. Jasper, Dezzarae Luera, Shiwen Luo, Hai Rao

Research output: Contribution to journalArticlepeer-review


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).

Original languageEnglish (US)
Pages (from-to)254-258
Number of pages5
JournalBiochemical and Biophysical Research Communications
Issue number1
StatePublished - Jan 29 2020
Externally publishedYes


  • Atg9
  • Autophagy
  • Proteasome
  • Protein degradation
  • Stress response

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


Dive into the research topics of 'Autophagy regulator Atg9 is degraded by the proteasome'. Together they form a unique fingerprint.

Cite this