Ubap2, or Ubiquitin-associated protein 2, is involved in multiple biological functions and pathways. It has been linked to processes like purine synthesis through its role in purinosome assembly [1]. Additionally, it participates in maintaining bone homeostasis by regulating osteoblastogenesis and osteoclastogenesis [2]. Genetic models, such as knockout (KO) mouse models, are valuable for studying Ubap2's functions.

In KO mouse models, pancreatic Ubap2 deletion affects glucose tolerance, inflammation, and provides protection from cerulein-induced pancreatitis. Mechanistically, it reduces NF-κB activation, cytokines, and tissue damage [3]. In hepatocellular carcinoma, knockdown of UBAP2 in vitro and in vivo impedes cancer development and reduces radiation resistance, revealing its role in promoting radioresistance through SLC27A5 ubiquitination [4].

In conclusion, Ubap2 is crucial for processes like purine synthesis, bone homeostasis, and has implications in diseases such as pancreatitis and hepatocellular carcinoma. Mouse KO models have been instrumental in uncovering its functions in these specific biological processes and disease conditions, providing insights into potential therapeutic targets.

References:

1. Chou, Ming-Chieh, Wang, Yi-Hsuan, Chen, Fei-Yun, Huang, Jie-Rong, Chen, Ruey-Hwa. 2023. PAICS ubiquitination recruits UBAP2 to trigger phase separation for purinosome assembly. In Molecular cell, 83, 4123-4140.e12. doi:10.1016/j.molcel.2023.09.028. https://pubmed.ncbi.nlm.nih.gov/37848033/

2. Kim, Jeonghyun, Kim, Bo-Young, Lee, Jeong-Soo, Chung, Yoon-Sok, Jeong, Seon-Yong. 2023. UBAP2 plays a role in bone homeostasis through the regulation of osteoblastogenesis and osteoclastogenesis. In Nature communications, 14, 3668. doi:10.1038/s41467-023-39448-8. https://pubmed.ncbi.nlm.nih.gov/37339951/

3. Roy, Ram Vinod, Means, Nicolas, Rao, Geeta, Bhattacharya, Resham, Mukherjee, Priyabrata. 2023. Pancreatic Ubap2 deletion regulates glucose tolerance, inflammation, and protection from cerulein-induced pancreatitis. In Cancer letters, 578, 216455. doi:10.1016/j.canlet.2023.216455. https://pubmed.ncbi.nlm.nih.gov/37865160/

4. Liu, Zijian, Yuan, Jingsheng, Zeng, Qiwen, Wu, Zhenru, Han, Jiaqi. 2024. UBAP2 contributes to radioresistance by enhancing homologous recombination through SLC27A5 ubiquitination in hepatocellular carcinoma. In Biochimica et biophysica acta. Molecular basis of disease, 1870, 167481. doi:10.1016/j.bbadis.2024.167481. https://pubmed.ncbi.nlm.nih.gov/39186963/