# When the chains do not break: the role of USP10 in physiology and pathology

## TL;DR

This review explores the role of USP10, a deubiquitinase enzyme, in normal cellular functions and its involvement in diseases like cancer and neurodegeneration.

## Contribution

The paper provides a comprehensive overview of recent findings on USP10's physiological and pathological roles.

## Key findings

- USP10 is crucial for maintaining cellular function through deubiquitination.
- USP10 is implicated in cancer and neurodegenerative diseases.
- Modulating USP10 activity is being explored as a therapeutic strategy.

## Abstract

Deubiquitination is now understood to be as important as its partner ubiquitination for the maintenance of protein half-life, activity, and localization under both normal and pathological conditions. The enzymes that remove ubiquitin from target proteins are called deubiquitinases (DUBs) and they regulate a plethora of cellular processes. DUBs are essential enzymes that maintain intracellular protein homeostasis by recycling ubiquitin. Ubiquitination is a post-translational modification where ubiquitin molecules are added to proteins thus influencing activation, localization, and complex formation. Ubiquitin also acts as a tag for protein degradation, especially by proteasomal or lysosomal degradation systems. With ~100 members, DUBs are a large enzyme family; the ubiquitin-specific peptidases (USPs) being the largest group. USP10, an important member of this family, has enormous significance in diverse cellular processes and many human diseases. In this review, we discuss recent studies that define the roles of USP10 in maintaining cellular function, its involvement in human pathologies, and the molecular mechanisms underlying its association with cancer and neurodegenerative diseases. We also discuss efforts to modulate USPs as therapy in these diseases.