Ubxn2a, a ubiquitin-like protein, has been shown to play crucial roles in multiple biological processes. It is involved in regulating protein turnover within key signaling pathways, and is particularly important in cancer-related processes. Its functions are associated with pathways such as the mTORC2 signaling pathway, which is relevant to tumor progression, as well as processes related to the regulation of oncoproteins [1,2]. Genetic models, especially mouse models, have been valuable in studying its functions [1].

In murine models, haploinsufficiency of UBXN2A significantly increases colon tumorigenesis, indicating its role as a potential tumor suppressor [1]. UBXN2A targets Rictor, a key component of the mTORC2 complex, for 26S proteasomal degradation, thus suppressing the Rictor-mTORC2 signaling pathway [1]. This leads to reduced AKT phosphorylation downstream of the mTORC2 pathway, affecting cellular processes like cell migration [1]. Additionally, studies in mice have shown that UBXN2A enhances CHIP-mediated proteasomal degradation of the oncoprotein mortalin-2 (mot-2) in colon tissues [3].

In conclusion, Ubxn2a has essential functions in regulating protein degradation and signaling pathways. Mouse models, especially those with Ubxn2a haploinsufficiency, have revealed its significance in colon cancer development, highlighting its potential as a therapeutic target in colorectal cancer [1,3].