Ubiquitin-Conjugating Enzyme E2T (UBE2T), also known as HSPC150, is a member of the ubiquitin-conjugating enzyme family. These enzymes play a crucial role in the ubiquitination process, which tags proteins for degradation via the proteasome. UBE2T is involved in various cellular processes, including cell cycle regulation, DNA repair, and signal transduction.
UBE2T contains a typical UBC domain, which allows it to interact with E3 ligases, such as the RING finger or HECT domain-containing proteins. This interaction facilitates the transfer of ubiquitin from the E2 enzyme to the substrate protein, leading to its mono- or polyubiquitination . UBE2T was initially identified as a key player in the Fanconi anemia (FA) pathway, where it is involved in DNA repair .
UBE2T has been implicated in various types of cancer, acting as an oncogene. It promotes tumor growth and progression by regulating the ubiquitination and degradation of tumor suppressor proteins. For instance, UBE2T has been shown to interact with the BRCA1/BARD1 complex, leading to the ubiquitination and downregulation of BRCA1 in breast cancer cells . This interaction is critical for the development and progression of breast cancer.
In lung adenocarcinoma, UBE2T promotes autophagy via the p53/AMPK/mTOR signaling pathway . Overexpression of UBE2T has been associated with increased proliferation and autophagy in lung cancer cells, contributing to drug resistance and poor prognosis .
The clinical relevance of UBE2T extends beyond its role in cancer. Its expression levels and activity can serve as potential biomarkers for cancer diagnosis and prognosis. Additionally, targeting UBE2T and its associated pathways may offer new therapeutic strategies for cancer treatment.