Structure and function of USP5: Insight into physiological and pathophysiological roles.

Area of Science:

• Biochemistry and Molecular Biology
• Cellular Biology
• Enzymology

Background:

• Deubiquitinases (DUBs) are critical enzymes that remove ubiquitin chains from proteins, influencing DNA repair, protein stability, and localization.
• The ubiquitin-specific proteinase (USP) family constitutes the largest class of DUBs.
• Ubiquitin-specific proteinase 5 (USP5) uniquely recognizes unanchored polyubiquitin and is vital for monoubiquitin pool homeostasis.

Purpose of the Study:

• To provide a comprehensive review of ubiquitin-specific proteinase 5 (USP5).
• To elucidate the structure, physiological functions, and pathophysiological roles of USP5.
• To explore USP5's involvement in diseases, particularly cancer, and its therapeutic potential.

Main Methods:

• Literature review synthesizing current knowledge on USP5.
• Analysis of USP5's structural and sequence homology within the DUB family.
• Examination of USP5's involvement in various cellular events and disease pathways.

Main Results:

• USP5 possesses unique ubiquitin-binding capabilities and is essential for maintaining cellular ubiquitin balance.
• USP5 plays significant roles in diverse cellular processes, including DNA repair and protein regulation.
• Dysregulation of USP5 is implicated in various diseases, notably cancer, suggesting its potential as a therapeutic target.

Conclusions:

• USP5 is a critical deubiquitinase with broad physiological and pathophysiological implications.
• Understanding USP5's signaling pathways and pharmacological profiles offers therapeutic avenues for cancer and neurological disorders.
• USP5 represents a promising target for developing novel treatments for a range of human diseases.