4.5 Article

Tor and the Sin3-Rpd3 complex regulate expression of the mitophagy receptor protein Atg32 in yeast

期刊

JOURNAL OF CELL SCIENCE
卷 127, 期 14, 页码 3184-3196

出版社

COMPANY BIOLOGISTS LTD
DOI: 10.1242/jcs.153254

关键词

Autophagy; Mitophagy; Mitochondria; Yeast; Atg32; Tor; Sin3; Rpd3

资金

  1. Ministry of Education, Culture, Sports, Science, and Technology (MEXT) program 'Promotion of Environmental Improvement for Independence of Young Researchers' under the Special Coordination Funds for Promoting Science and Technology
  2. Japan Society for the Promotion of Science KAKENHI [23689032, 25117714, 25560414, 26291039, 6660061, 26111511, 26292052, 26850064]
  3. Japan Science and Technology Agency [3580]
  4. Uehara Memorial Foundation
  5. Tokyo Biochemical Research Foundation
  6. Suzuken Memorial Foundation
  7. Grants-in-Aid for Scientific Research [25560414, 26292052, 26111511, 25461212, 26850064, 26291039, 13J04836, 25117714, 24590387] Funding Source: KAKEN

向作者/读者索取更多资源

When mitophagy is induced in Saccharomyces cerevisiae, the mitochondrial outer membrane protein ScAtg32 interacts with the cytosolic adaptor protein ScAtg11. ScAtg11 then delivers the mitochondria to the pre-autophagosomal structure for autophagic degradation. Despite the importance of ScAtg32 for mitophagy, the expression and functional regulation of ScAtg32 are poorly understood. In this study, we identified and characterized the ScAtg32 homolog in Pichia pastoris (PpAtg32). Interestingly, we found that PpAtg32 was barely expressed before induction of mitophagy and was rapidly expressed after induction of mitophagy by starvation. Additionally, PpAtg32 was phosphorylated when mitophagy was induced. We found that PpAtg32 expression was suppressed by Tor and the downstream PpSin3-PpRpd3 complex. Inhibition of Tor by rapamycin induced PpAtg32 expression, but could neither phosphorylate PpAtg32 nor induce mitophagy. Based on these findings, we conclude that the Tor and PpSin3-PpRpd3 pathway regulates PpAtg32 expression, but not PpAtg32 phosphorylation.

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