Ubiquitin Conjugating Enzyme E2S (UBE2S) is a member of the ubiquitin-conjugating enzyme family, also known as E2 enzymes. These enzymes play a crucial role in the ubiquitination process, which is essential for protein degradation and regulation within the cell. UBE2S is particularly significant due to its involvement in various cellular processes, including cell cycle regulation, DNA repair, and signal transduction.
UBE2S is characterized by its ability to receive ubiquitin from a ubiquitin-activating enzyme (E1) and subsequently interact with a ubiquitin ligase (E3) to conjugate ubiquitin to substrate proteins . This process is vital for targeting proteins for degradation via the proteasome, thus maintaining protein homeostasis within the cell .
The ubiquitin-proteasome system (UPS) orchestrates the specific poly-ubiquitination of protein substrates in humans, which can lead to their degradation . UBE2S, as part of this system, ensures the proper turnover of proteins, preventing the accumulation of damaged or misfolded proteins that could potentially lead to cellular dysfunction and disease.
Recombinant human UBE2S is produced using recombinant DNA technology, which involves inserting the gene encoding UBE2S into a suitable expression system, such as bacteria or yeast. This allows for the large-scale production of UBE2S, which can be used for various research and therapeutic purposes. Recombinant UBE2S retains the functional properties of the native enzyme, making it a valuable tool for studying the ubiquitination process and its implications in health and disease .
UBE2S is widely used in research to understand its role in the ubiquitination process and its impact on cellular functions. Studies have shown that UBE2S is involved in maintaining proteostasis during aging, ensuring protein quality control, and preventing the accumulation of poly-ubiquitinated proteins . These findings highlight the importance of UBE2S in cellular homeostasis and its potential as a therapeutic target for age-related diseases and other conditions associated with protein misfolding and aggregation.