USP37 Protein, Human (sf9, His)

The USP37 Protein, as delineated in this description, serves as a versatile deubiquitinase with significant roles in various cellular processes, including cell cycle regulation, DNA replication, and DNA damage response. During the G1/S transition, USP37 antagonizes the anaphase-promoting complex (APC/C) by mediating the deubiquitination of cyclin-A (CCNA1 and CCNA2), facilitating S phase entry. Phosphorylation at Ser-628 during G1/S phase enhances its deubiquitinase activity, preventing the degradation of cyclin-A. USP37 further contributes to DNA replication by stabilizing the licensing factor CDT1 and promoting the efficiency and fidelity of replication by deubiquitinating checkpoint kinase 1/CHK1. It sustains the DNA damage response by deubiquitinating and stabilizing the ATP-dependent DNA helicase BLM in the context of DNA double-strand breaks. Additionally, USP37 plays a role in promoting cell migration by deubiquitinating and stabilizing the epithelial-mesenchymal transition (EMT)-inducing transcription factor SNAI. Its involvement in the regulation of mitotic spindle assembly and mitotic progression is highlighted by its association with chromatin-associated WAPL, stabilizing it through deubiquitination. The multifaceted functions of USP37 underscore its importance in coordinating critical cellular events.