Fubp3-KO Mouse

Fubp3, the far upstream element-binding protein 3, is involved in multiple biological functions and pathways. It acts as a transcription factor and is associated with immune-related responses, cell proliferation, and viral-host interactions. For example, it may play a role in neuron-mediated immune responses and is involved in pathways related to the progression of chronic myeloid leukaemia and the replication of certain viruses [1,2,3]. Genetic models, such as gene knockout (KO) or conditional knockout (CKO) mouse models, could potentially be valuable for further understanding its functions.

In Alzheimer's disease, Fubp3 was found to mediate amyloid-β-induced neuronal NLRP3 expression. In primary neurons and a neuroblastoma cell line, Fubp3 was required for endogenous NLRP3 expression and tau phosphorylation only in the presence of amyloid-β. Its expression was markedly increased in cortical neurons of aged wild-type mice and an Alzheimer's disease mouse model [1]. In chronic myeloid leukaemia, microdeletions of the Fubp3 gene and its reduced expression were associated with poor prognostic markers. Decrease in FUBP3 protein in K562 cells led to increased proliferation and survival due to MAPK-ERK pathway activation [2]. In porcine epidemic diarrhea virus (PEDV) infection, FUBP3 suppressed PEDV replication by degrading the viral nucleocapsid protein via selective autophagy and positively regulated type-I interferon signaling [3]. In Japanese encephalitis virus (JEV) infection, knockdown of FUBP3 protein decreased JEV viral titer, while its overexpression increased viral infectivity, suggesting it regulates JEV RNA replication [4].

In conclusion, Fubp3 has diverse functions in different biological processes and disease conditions. Studies in model systems, including those related to Alzheimer's disease, chronic myeloid leukaemia, and viral infections, have revealed its importance in immune-related responses, disease progression, and viral replication. These findings highlight the potential of Fubp3 as a therapeutic target in these disease areas.

References:

1. Yao, Jing, Li, Yuan, Liu, Xi, Wang, Zhe, Song, Weihong. 2024. FUBP3 mediates the amyloid-β-induced neuronal NLRP3 expression. In Neural regeneration research, 20, 2068-2083. doi:10.4103/NRR.NRR-D-23-01799. https://pubmed.ncbi.nlm.nih.gov/39254567/

2. Sharma, Mugdha, Anandram, Seetharam, Ross, Cecil, Srivastava, Sweta. 2022. FUBP3 regulates chronic myeloid leukaemia progression through PRC2 complex regulated PAK1-ERK signalling. In Journal of cellular and molecular medicine, 27, 15-29. doi:10.1111/jcmm.17584. https://pubmed.ncbi.nlm.nih.gov/36478132/

3. Dong, Sujie, Kong, Ning, Wang, Chunmei, Tong, Guangzhi, Shan, Tongling. 2022. FUBP3 Degrades the Porcine Epidemic Diarrhea Virus Nucleocapsid Protein and Induces the Production of Type I Interferon. In Journal of virology, 96, e0061822. doi:10.1128/jvi.00618-22. https://pubmed.ncbi.nlm.nih.gov/35695513/

4. Xu, Peng, Tong, Wei, Chen, Young-Mao. 2021. FUSE binding protein FUBP3 is a potent regulator in Japanese encephalitis virus infection. In Virology journal, 18, 224. doi:10.1186/s12985-021-01697-8. https://pubmed.ncbi.nlm.nih.gov/34794468/