Atg1 phosphorylation is activated by AMPK and indispensable for autophagy induction in insects
文献类型： 外文期刊
作者： Zhao, Haigang 1 ; Long, Shihui 1 ; Liu, Suning 1 ; Yuan, Dongwei 1 ; Huang, Danyan 1 ; Xu, Jing 2 ; Ma, Qiuqin 2 ; Wang, Guirong 6 ; Wang, Jian 7 ; Li, Sheng 1 ; Tian, Ling 2 ; Li, Kang 1 ;
作者机构： 1.South China Normal Univ, Inst Insect Sci & Technol, Sch Life Sci, Guangdong Prov Key Lab Insect Dev Biol & Appl Tech, Guangzhou 510631, Peoples R China
2.South China Agr Univ, Coll Anim Sci, Guangdong Lab Lingnan Modern Agr, Guangdong Prov Key Lab Agroanim Genom & Mol Breedi, Guangzhou 510642, Peoples R China
3.Chinese Acad Sci, Inst Plant Physiol & Ecol, Key Lab Dev & Evolutionary Biol, Shanghai 200032, Peoples R China
4.Univ Chinese Acad Sci, Beijing 100049, Peoples R China
5.South China Normal Univ, Guangmeiyuan R&D Ctr, Guangdong Prov Key Lab Insect Dev Biol & Appl Tech, Meizhou 514779, Peoples R China
6.Chinese Acad Agr Sci, Agr Genom Inst Shenzhen, Shenzhen Branch, Guangdong Lab Lingnan Modern Agr,Genome Anal Lab M, Shenzhen 518120, Peoples R China
7.Univ Maryland, Dept Entomol, College Pk, MD 20742 USA
8.South China Univ Technol, Sch Food Sci & Engn, Guangzhou 510641, Peoples R China
9.ChemPartner PharmaTech Co Ltd, Jiangmen 529081, Peoples R China
10.Quantum Hitech Guangdong Biol Co Ltd, Jiangmen 529081, Peoples R China
关键词： Autophagy; BmAtg1c; DmAtg1; AMPK; Phosphorylation modification; Starvation; 20-Hydroxyecdysone
期刊名称：INSECT BIOCHEMISTRY AND MOLECULAR BIOLOGY （ 影响因子：4.421； 五年影响因子：4.774 ）
ISSN： 0965-1748
年卷期： 2023 年 152 卷
页码：
收录情况： SCI
摘要： Phosphorylation is a key post-translational modification in regulating autophagy in yeast and mammalians, yet it is not fully illustrated in invertebrates such as insects. ULK1/Atg1 is a functionally conserved serine/threonine protein kinase involved in autophagosome initiation. As a result of alternative splicing, Atg1 in the silkworm, Bombyx mori, is present as three mRNA isoforms, with BmAtg1c showing the highest expression levels. Here, we found that BmAtg1c mRNA expression, BmAtg1c protein expression and phosphorylation, and autophagy simultaneously peaked in the fat body during larval-pupal metamorphosis. Importantly, two BmAtg1c phos-phorylation sites were identified at Ser269 and Ser270, which were activated by BmAMPK, the major energy -sensing kinase, upon stimulation with 20-hydroxyecdysone and starvation; additionally, these Atg1 phosphor-ylation sites are evolutionarily conserved in insects. The two BmAMPK-activated phosphorylation sites in BmAtg1c were found to be required for BmAMPK-induced autophagy. Moreover, the two corresponding DmAtg1 phosphorylation sites in the fruit fly, Drosophila melanogaster, are functionally conserved for autophagy induc-tion. In conclusion, AMPK-activated Atg1 phosphorylation is indispensable for autophagy induction and evolutionarily conserved in insects, shedding light on how various groups of organisms differentially regulate ULK1/Atg1 phosphorylation for autophagy induction.
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