Small-molecule allosteric activator of ubiquitin-specific protease 7 (USP7)

Proc Natl Acad Sci U S A. 2025 Oct 21;122(42):e2510496122. doi: 10.1073/pnas.2510496122. Epub 2025 Oct 14.

Abstract

Ubiquitin-specific protease 7 (USP7) is a deubiquitylase essential for cell homeostasis, DNA repair, and regulation of both tumor suppressors and oncogenes. Recently, haploinsufficiency of USP7 has been associated with Hao-Fountain syndrome (HAFOUS), a rare neurodevelopmental disorder. Although a range of USP7 inhibitors have been developed over the last decade, in the context of HAFOUS, USP7 activators may represent a more relevant approach. To address this challenge, we report the identification and characterization of a small-molecule activator of USP7 called MS-8. Structural and functional studies show that MS-8 allosterically activates USP7, mimicking the endogenous autoactivation mechanism of the enzyme. We observed that MS-8 engages and activates mutant USP7 in a cellular context, impacting downstream proteins. Taken together, our study provides validation of the USP7 activator that paves the way toward activation-driven USP7 pharmacology.

Keywords: DUB; Hao–Fountain syndrome; USP7; deubiquitylases; small-molecule activator.

MeSH terms

  • Allosteric Regulation
  • Enzyme Activation / drug effects
  • Enzyme Activators* / chemistry
  • Enzyme Activators* / pharmacology
  • HEK293 Cells
  • Humans
  • Small Molecule Libraries* / chemistry
  • Small Molecule Libraries* / pharmacology
  • Ubiquitin-Specific Peptidase 7* / chemistry
  • Ubiquitin-Specific Peptidase 7* / genetics
  • Ubiquitin-Specific Peptidase 7* / metabolism

Substances

  • Ubiquitin-Specific Peptidase 7
  • USP7 protein, human
  • Small Molecule Libraries
  • Enzyme Activators