| Autor: |
Zheng J; Department of Internal Medicine, Division of Hematology, Oncology, and Palliative Care, Massey Cancer Center, School of Medicine, Virginia Commonwealth University, Richmond, VA 23298, USA.; Department of Obstetrics and Gynecology, Li Ka Shing Faculty of Medicine, The University of Hong Kong, Hong Kong 999077, China., Chen C; Department of Bioengineering, School of Engineering, Virginia Commonwealth University, Richmond, VA 23298, USA., Guo C; Department of Human and Molecular Genetics, School of Medicine, Virginia Commonwealth University, Richmond, VA 23298, USA., Caba C; Department of Chemistry and Biochemistry, University of Windsor, Windsor, ON N9B 3P4, Canada., Tong Y; Department of Chemistry and Biochemistry, University of Windsor, Windsor, ON N9B 3P4, Canada., Wang H; Department of Internal Medicine, Division of Hematology, Oncology, and Palliative Care, Massey Cancer Center, School of Medicine, Virginia Commonwealth University, Richmond, VA 23298, USA. |
| Abstrakt: |
Ubiquitin-specific peptidase 16 (USP16) is a deubiquitinase that plays a role in the regulation of gene expression, cell cycle progression, and various other functions. It was originally identified as the major deubiquitinase for histone H2A and has since been found to deubiquitinate a range of other substrates, including proteins from both the cytoplasm and nucleus. USP16 is phosphorylated when cells enter mitosis and dephosphorylated during the metaphase/anaphase transition. While much of USP16 is localized in the cytoplasm, separating the enzyme from its substrates is considered an important regulatory mechanism. Some of the functions that USP16 has been linked to include DNA damage repair, immune disease, tumorigenesis, protein synthesis, coronary artery health, and male infertility. The strong connection to immune response and the fact that multiple oncogene products are substrates of USP16 suggests that USP16 may be a potential therapeutic target for the treatment of certain human diseases. |
