Acetylation of BmAtg8 inhibits starvation-induced autophagy initiation

Xue, Shifeng; Mao, Fuxiang; Hu, Dongbing; Yan, Huihui; Lei, Jihai; Obeng, Enoch; Zhou, Yuefan; Quan, Yanping; Yu, Wengong

doi:10.1007/s11010-019-03513-y

Cited by 12 publications

(10 citation statements)

References 44 publications

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“…In B. mori, 20E and its precursor cholesterol both induce dephosphorylation of BmHDAC1 and its nucleo-cytoplasmic translocation to promote autophagy, while the functional mechanism of BmHDAC1 in regulating autophagy is lack of investigation (Wu et al, 2021b). It is reported that the lysine site K13 of BmAtg8 protein is acetylated after BmNPV infection, and acetylation-mimic mutation of K13 in BmAtg8 significantly reduces autophagy (Xue et al, 2019). In order to fully understand the regulation of autophagy by acetylation in silkworm, an in-depth study of the molecular components BmAtg3, BmAtg4, BmAtg7, and BmAtg8 from BmAtg8-PE ubiquitin-like protein system has been performed.…”

Section: Acetylationmentioning

confidence: 99%

Transcription and Post-translational Regulation of Autophagy in Insects

Xiao

et al. 2022

Front. Physiol.

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Autophagy attracts great attention, and numerous progresses have been obtained in the last two decades. Autophagy is implicated in mammalian neurodegenerative diseases, tumorigenesis, as well as development in insects. The regulatory mechanism of autophagy is well documented in yeast and mammals, whereas it is not fully illustrated in insects. Drosophila melanogaster and Bombyx mori are the two well-studied insects for autophagy, and several insect-mammalian evolutionarily conserved or insect-specific mechanisms in regulating autophagy are reported. In this review, we summarize the most recent studies of autophagy regulated at both transcriptional and post-translational levels by insect hormone in cooperation with other signals, such as nutrient, which will provide a reference and deep thinking for studies on autophagy in insects.

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Section: Acetylationmentioning

confidence: 99%

Transcription and Post-translational Regulation of Autophagy in Insects

Xiao

et al. 2022

Front. Physiol.

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“…Currently, several acetylated silkworm proteins involved in the cellular regulation process during BmNPV infection have been studied in our laboratory, including the heat shock response (Mao et al, 2021), autophagy (Xue et al, 2019), and apoptosis (Zhou et al, 2016) proteins. Apoptosis is an important antivirus defense due to its impact on virus multiplication and pathogenesis, and a host inhibitor of apoptosis proteins (IAPs) may function as critical sentinels of virus invasion in insects.…”

Section: Introductionmentioning

confidence: 99%

Deacetylation of BmAda3 is required for cell apoptosis caused by Bombyx mori nucleopolyhedrovirus infection

Zhu

Ngowo

et al. 2021

Arch Insect Biochem Physiol

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Silkworm is not only an ideal insect model with a biological significance, but it is also crucially important in sericulture and bioreactors. Bombyx mori nucleopolyhedrovirus (BmNPV) is a principal pathogen of silkworm. However, the molecular mechanism underlying BmNPV invasion is still unclear. Based on our previous acetylome research findings of B. mori after BmNPV infection, here, we focused on silkworm alteration/deficiency in activation‐3 (BmAda3). The acetylation of K124 and K128 were significantly reduced (0.66‐fold) upon the virus challenge. Due to the interaction between Ada3 and P53, acetylation‐mimic K124Q/K128Q and deacetylation‐mimic K124R/K128R mutants of BmAda3 were constructed to explore the roles exerted by the acetylation modification of BmAda3 on P53. Yeast two‐hybrid and IP results revealed that both BmAda3 and its deacetylation mutants (K124R/K128R) interacted with P53. Interestingly, we found that the deacetylation mutants (K124R/K128R) of BmAda3 significantly promoted the stability of P53. Since P53 is a proapoptotic factor, cell apoptosis was detected. We established that the deacetylation of BmAda3 at K124/K128 facilitated cellular apoptosis during BmNPV infection. Finally, viral proliferation was analyzed, and the results indicated that virus generation was reduced by K124/K128 deacetylation. Our report, based on the deacetylation of two lysine sites 124/128 of BmAda3, shows possible regulatory pathways of BmNPV proliferation and provides novel insights into the development of antiviral agents.

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“…Bombyx mori CREB binding protein (BmCBP) was found to acetylate H3K27, which is involved in the expression of Bombyx mori CCAAT/enhancer‐binding protein gamma (BmC/EBPg) (Lyu et al, 2020). Additionally, acetylation can regulate the response of BmN cells to Bombyx mori nucleopolyhedrovirus (BmNPV) infection (Hu et al, 2018; Xue et al, 2019). In our previous work, a high‐throughput determination of acetylated proteins in silkworm was conducted by nanospray high‐performance liquid chromatography/tandem mass spectrometry (nano‐HPLC/MS/MS) technology, and a large number of acetylated nutrient storage proteins were identified (Nie et al, 2015).…”

Section: Introductionmentioning

confidence: 99%

The acetylation modification regulates the stability of Bm30K‐15 protein and its mechanism in silkworm, Bombyx mori

Liu

et al. 2021

Arch Insect Biochem Physiol

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The 30 K proteins are the major silkworm hemolymph proteins and are involved in a variety of physiological processes, such as nutrient and energy storage, embryogenesis, immune response, and inhibition of apoptosis. The Bm30K‐15 protein is one of the 30 K proteins and is abundant in the hemolymph of fifth instar silkworm larva. We previously found that the Bm30K‐15 protein can be acetylated. In the present study, we found that acetylation can improve the protein stability of Bm30K‐15. Further exploration confirmed that the increase in protein stability by acetylation was caused by competition between acetylation and ubiquitination. In summary, these findings aim to provide insight into the effect of acetylation modification on the protein level and stability of the Bm30K‐15 and the possible molecular mechanism of its existence in silkworm, Bombyx mori.

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Acetylation of BmAtg8 inhibits starvation-induced autophagy initiation

Cited by 12 publications

References 44 publications

Transcription and Post-translational Regulation of Autophagy in Insects

Transcription and Post-translational Regulation of Autophagy in Insects

Deacetylation of BmAda3 is required for cell apoptosis caused by Bombyx mori nucleopolyhedrovirus infection

The acetylation modification regulates the stability of Bm30K‐15 protein and its mechanism in silkworm, Bombyx mori

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