Trim75, a member of the RING E3 ligase family, plays a vital role in protein ubiquitination, which controls intracellular protein degradation and regulates cell signaling pathways [2]. Protein ubiquitination is a key process in many biological functions, making Trim75 potentially significant in multiple biological processes. Mouse models are valuable genetic models for studying Trim75.

In mouse early embryos, Trim75 is a maternal factor that contributes to the zygotic genome activation (ZGA) program. It may be a potential driver of minor ZGA, recruiting EP300 and establishing H3K27ac in the gene body of minor ZGA genes, thus facilitating mammalian preimplantation embryo development [1]. In studies of mouse oocytes, peptide nanoparticle-mediated siRNA transfection was used to knock down Trim75, achieving the expected meiotic phenotypes, which suggests that peptide nanoparticles may be superior for preliminary functional studies of unknown genes in mouse oocytes [3]. Additionally, in a study of mouse models of dystrophinopathy, Trim75 was identified as a candidate E3 ligase that may specifically regulate dystrophin protein turnover in vivo [4].

In conclusion, Trim75 is crucial for early embryo development in mice through its role in ZGA. Its function in regulating protein turnover, as seen in the context of dystrophinopathy, also indicates its importance in muscle-related biological processes. The use of mouse models, especially those involving gene knockdown or knockout, has been instrumental in uncovering these functions, providing insights into potential disease mechanisms related to embryo development and muscle-associated diseases.

References:

1. Hou, Weibo, Chen, Lijun, Ji, Jingzhang, Cai, Wenpin, Yang, Xu. 2024. Maternal factor Trim75 contributes to zygotic genome activation program in mouse early embryos. In Molecular biology reports, 51, 560. doi:10.1007/s11033-024-09349-0. https://pubmed.ncbi.nlm.nih.gov/38643284/

2. Lou, Xiaohua, Ma, Binbin, Zhuang, Yuan, Zhang, Zhiqiang, Li, Xian C. 2022. Structural studies of the coiled-coil domain of TRIM75 reveal a tetramer architecture facilitating its E3 ligase complex. In Computational and structural biotechnology journal, 20, 4921-4929. doi:10.1016/j.csbj.2022.08.069. https://pubmed.ncbi.nlm.nih.gov/36147661/

3. Jin, Zhen, Li, Ruichao, Zhou, Chunxiang, Yang, Zhixia, Zhang, Dong. 2016. Efficient Gene Knockdown in Mouse Oocytes through Peptide Nanoparticle-Mediated SiRNA Transfection. In PloS one, 11, e0150462. doi:10.1371/journal.pone.0150462. https://pubmed.ncbi.nlm.nih.gov/26974323/

4. McCourt, Jackie L, Talsness, Dana M, Lindsay, Angus, Lowe, Dawn A, Ervasti, James M. . Mouse models of two missense mutations in actin-binding domain 1 of dystrophin associated with Duchenne or Becker muscular dystrophy. In Human molecular genetics, 27, 451-462. doi:10.1093/hmg/ddx414. https://pubmed.ncbi.nlm.nih.gov/29194514/