2. Academic Validation
  3. BmCBP Catalyzes the Acetylation of BmApoLp-II Protein and Regulates Its Stability in Silkworm, Bombyx mori

BmCBP Catalyzes the Acetylation of BmApoLp-II Protein and Regulates Its Stability in Silkworm, Bombyx mori

  • Insects. 2023 Mar 23;14(4):309. doi: 10.3390/insects14040309.
Yanmei Chen 1,  Jiao Lv 1,  Guowei Zu 1,  Fan Yang 1,  Jiasheng Geng 1,  Zhengying You 1,  Caiying Jiang 1,  Qing Sheng 1,  Zuoming Nie 1
Affiliations

Affiliation

  • 1 Zhejiang Provincial Key Laboratory of Silkworm Bioreactor and Biomedicine, College of Life Sciences and Medicine, Zhejiang Sci-Tech University, Hangzhou 310018, China.
PMID: 37103124 DOI: 10.3390/insects14040309
Abstract

Acetylation is an important and reversible post-translational modification (PTM) of protein, which is involved in many cellular physiological processes. In previous studies, lots of nutrient storage proteins were found to be highly acetylated in silkworms, and acetylation can improve the stability of these proteins. However, the related acetyltransferase was not involved. In the present work, a Bombyx mori nutrient storage protein, apolipophorin II (BmApoLp-II), was further confirmed to be acetylated, and the acetylation could improve its protein expression. Furthermore, RNAi and Co-IP showed that the acetyltransferase BmCBP was found to catalyze the acetylation modification of BmApoLp-II, and thus affect its protein expression. Meanwhile, it was proved that acetylation could improve the stability of the BmApoLp-II protein by completing its ubiquitination. These results lay a foundation for further study on the mechanism of regulating nutrition storage and hydrolysis utilization of storage proteins by BmCBP and the acetylation in the silkworm Bombyx mori.

Keywords

BmApoLp-II; BmCBP; Bombyx mori; acetylation; protein stability.

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