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Cholesterol derivatives induce dephosphorylation of the histone deacetylases Rpd3/HDAC1 to upregulate autophagy

文献类型： 外文期刊

作者： Wu, Wenmei 1 ; Luo, Man 1 ; Li, Kang 3 ; Dai, Yichen 1 ; Yi, Huiyu 1 ; Zhong, Yangjin 1 ; Cao, Yang 1 ; Tettamanti, Gianl 1 ;

作者机构： 1.South China Agr Univ, Coll Anim Sci, Guangdong Lab Lingnan Modern Agr, Guangdong Prov Key Lab Agroanim Genom & Mol Breed, Guangzhou, Peoples R China

2.South China Agr Univ, Coll Anim Sci, Guangdong Prov Sericulture & Mulberry Engn Res Ct, Guangzhou, Peoples R China

3.South China Normal Univ, Inst Insect Sci & Technol, Sch Life Sci, Guangdong Prov Key Lab Insect Dev Biol & Appl Tec, Guangzhou, Peoples R China

4.Southwest Univ, Biol Sci Res Ctr, Chongqing Engn & Technol Res Ctr Novel Silk Mat, Chongqing, Peoples R China

5.Univ Insubria, Dept Biotechnol & Life Sci, Varese, Italy

关键词： Autophagy; BmRpd3; HsHDAC1; cholesterol derivatives; dephosphorylation; nucleo-cytoplasmic translocation; MTOR

期刊名称：AUTOPHAGY （ 影响因子：16.016； 五年影响因子：16.586 ）

ISSN： 1554-8627

年卷期：

页码：

收录情况： SCI

摘要： Histone deacetylases (HDACs) are important for global gene expression and contribute to numerous physiological events. Deacetylase Rpd3 in yeast and its conserved homolog HDAC1 in mammals oppositely regulate autophagy; however, how Rpd3/HDAC1 is regulated to mediate autophagy remains unclear. Here, we showed autophagy occurrence in silkworm (Bombyx mori) required BmRpd3, wherein steroid hormone 20-hydroxyecdysone (20E) signaling regulated its protein level and nuclear localization negatively. Inhibition of MTOR led to dephosphorylation and nucleo-cytoplasmic translocation of BmRpd3/HsHDAC1. Besides, cholesterol, 20E, and 27-hydroxycholesterol could all induce massive dephosphorylation and cytoplasmic localization of BmRpd3/HsHDAC1, and thus autophagy by affecting MTORC1 activity. In addition, three phosphorylation sites (Ser392, Ser421, and Ser423) identified in BmRpd3 were conserved in HsHDAC1. Single or triple phosphorylation-site mutation attenuated the phosphorylation levels of BmRpd3/HsHDAC1, leading to their cytoplasmic localization and autophagy activation. In general, cholesterol derivatives, especially hydroxylated cholesterol, caused dephosphorylation and nucleo-cytoplasmic shuttling of BmRpd3/HsHDAC1 through inhibition of MTOR signaling to facilitate autophagy in B. mori and mammals. These findings improve our understandings of BmRpd3/HsHDAC1-mediated autophagy induced by cholesterol derivatives and shed light on their potential as a therapeutic target for neurodegenerative diseases and autophagy-related studies.

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