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Biochem Biophys Res Commun. 2019 Apr 2;511(2):434-439. doi: 10.1016/j.bbrc.2019.02.077. Epub 2019 Feb 21.

TORC1 regulates autophagy induction in response to proteotoxic stress in yeast and human cells.

Author information

1
Department of Biological Science, Shizuoka University, Shizuoka, 422-8021, Japan.
2
Course of Biological Science, Department of Science, Graduate School of Integrated Science and Technology, Shizuoka University, Shizuoka, 422-8021, Japan.
3
Biozentrum, University of Basel, 4056, Basel, Switzerland, Switzerland.
4
Biosignal Research Center, Kobe University, Kobe, 657-8501, Japan.
5
Department of Biology, Hamamatsu University School of Medicine, Hamamatsu, Shizuoka, 431-3192, Japan.
6
Department of Biological Science, Shizuoka University, Shizuoka, 422-8021, Japan; Course of Biological Science, Department of Science, Graduate School of Integrated Science and Technology, Shizuoka University, Shizuoka, 422-8021, Japan. Electronic address: ushimaru.takashi@shizuoka.ac.jp.

Abstract

Misfolded and aggregated proteins are eliminated to maintain protein homeostasis. Autophagy contributes to the removal of protein aggregates. However, if and how proteotoxic stress induces autophagy is poorly understood. Here we show that proteotoxic stress after treatment with azetidine-2-carboxylic acid (AZC), a toxic proline analog, induces autophagy in budding yeast. AZC treatment attenuated target of rapamycin complex 1 (TORC1) activity, resulting in the dephosphorylation of Atg13, a key factor of autophagy. By contrast, AZC treatment did not affect target of rapamycin complex 2 (TORC2). Proteotoxic stress also induced TORC1 inactivation and autophagy in fission yeast and human cells. This study suggested that TORC1 is a conserved key factor to cope with proteotoxic stress in eukaryotic cells.

KEYWORDS:

Autophagy; Azetidine-2-carboxylic acid (AZC); Proteotoxic stress; Target of rapamycin complex 1 (TORC1)

PMID:
30797551
DOI:
10.1016/j.bbrc.2019.02.077

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