The emerging role of USP29 in cancer and other diseases

Reversible protein ubiquitination is a key process for maintaining cellular homeostasis. Deubiquitinases, which can cleave ubiquitin from substrate proteins, have been reported to be deeply involved in disease progression ranging from oncology to neurological diseases. The human genome encodes approximately 100 deubiquitinases, most of which are poorly characterized. One of the well-characterized deubiquitases is ubiquitin-specific protease 29 (USP29), which is often upregulated in pathological tissues and plays important roles in the progression of different diseases. Moreover, several studies have shown that deletion of Usp29 in mice does not cause visible growth and developmental defects, indicating that USP29 may be an ideal therapeutic target. In this review, we provide a comprehensive summary of the important roles and regulatory mechanisms of USP29 in cancer and other diseases, which may help us better understand its biological functions and improve future studies to construct suitable USP29-targeted therapy systems. Deubiquitinases are deeply involved in human diseases and targeting them provides new opportunities for patients. Many studies have revealed that deubiquitinase USP29 does not affect normal development, but plays an important role in human diseases, especially cancers. In this review, we first summarize the important roles and mechanisms of USP29 in cancer and other diseases, intending to provide potential implications for both basic science and clinical applications.