Histone deacetylase HDA-1 modulates mitochondrial stress response and longevity

Li-Wa Shao, Qi Peng, Mingyue Dong, Kaiyu Gao, Yumei Li, Yi Li, Chuan-Yun Li () and Ying Liu ()
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Li-Wa Shao: Institute of Molecular Medicine, Peking University
Qi Peng: Institute of Molecular Medicine, Peking University
Mingyue Dong: Institute of Molecular Medicine, Peking University
Kaiyu Gao: Institute of Molecular Medicine, Peking University
Yumei Li: Institute of Molecular Medicine, Peking University
Yi Li: Institute of Molecular Medicine, Peking University
Chuan-Yun Li: Institute of Molecular Medicine, Peking University
Ying Liu: Institute of Molecular Medicine, Peking University

Nature Communications, 2020, vol. 11, issue 1, 1-12

Abstract: Abstract The ability to detect, respond and adapt to mitochondrial stress ensures the development and survival of organisms. Caenorhabditis elegans responds to mitochondrial stress by activating the mitochondrial unfolded protein response (UPRmt) to buffer the mitochondrial folding environment, rewire the metabolic state, and promote innate immunity and lifespan extension. Here we show that HDA-1, the C. elegans ortholog of mammalian histone deacetylase (HDAC) is required for mitochondrial stress-mediated activation of UPRmt. HDA-1 interacts and coordinates with the genome organizer DVE-1 to induce the transcription of a broad spectrum of UPRmt, innate immune response and metabolic reprogramming genes. In rhesus monkey and human tissues, HDAC1/2 transcript levels correlate with the expression of UPRmt genes. Knocking down or pharmacological inhibition of HDAC1/2 disrupts the activation of the UPRmt and the mitochondrial network in mammalian cells. Our results underscore an evolutionarily conserved mechanism of HDAC1/2 in modulating mitochondrial homeostasis and regulating longevity.

Date: 2020
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DOI: 10.1038/s41467-020-18501-w

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