The effect of acetylation on the protein stability of BmApoLp-III in the silkworm, Bombyx mori.

Abstract:

:Acetylation is an important, reversible posttranslational modification to a protein. In a previous study, we found that there were a large number of acetylated sites in various nutrient storage proteins of the silkworm haemolymph. In this study, we confirmed that acetylation can affect the stability of nutrient storage protein Bombyx mori apolipophorin-III (BmApoLp-III). First, the expression of BmApoLp-III could be upregulated when BmN cells were treated with the deacetylase inhibitor panobinostat (LBH589); similarly, the expression was downregulated when the cells were treated with the acetylase inhibitor C646. Furthermore, the increase in acetylation by LBH589 could inhibit the degradation and improve the accumulation of BmApoLp-III in BmN cells treated with cycloheximide and MG132 respectively. Moreover, we found that an increase in acetylation could decrease the ubiquitination of BmApoLp-III and vice versa; therefore, we predicted that acetylation could improve the stability of BmApoLp-III by competing for ubiquitination and inhibiting the protein degradation pathway mediated by ubiquitin. Additionally, BmApoLp-III had an antiapoptosis function that increased after LBH589 treatment, which might have been due to the improved protein stability after acetylation. These results have laid the foundation for further study on the mechanism of acetylation in regulating the storage and utilization of silkworm nutrition.

journal_name

Insect Mol Biol

journal_title

Insect molecular biology

authors

Yang F,Zhu B,Liu J,Liu Y,Jiang C,Sheng Q,Qiu J,Nie Z

doi

10.1111/imb.12613

subject

Has Abstract

pub_date

2020-02-01 00:00:00

pages

104-111

issue

1

eissn

0962-1075

issn

1365-2583

journal_volume

29

pub_type

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