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Transient interdomain interactions in free USP14 shape its conformational ensemble.

Johannes Salomonsson1, Björn Wallner1, Linda Sjöstrand2

  • 1Department of Physics, Chemistry and Biology, Linköping University, Linköping, Sweden.

Protein Science : a Publication of the Protein Society
|April 8, 2024
PubMed
Summary
This summary is machine-generated.

Ubiquitin-specific protease 14 (USP14) regulates proteasome function. Transient interactions between its Ubl and USP domains influence proteasome binding, offering insights for therapeutic strategies.

Keywords:
DUBNMRSAXSmolecular modelingprotein dynamics

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Medicine

Background:

  • The deubiquitinase (DUB) ubiquitin-specific protease 14 (USP14) is a key regulator of proteasomal degradation and a potential therapeutic target.
  • USP14 has a dual domain structure (USP and ubiquitin-like domains) and its activity is modulated by proteasome binding.

Purpose of the Study:

  • To investigate the structural and dynamic roles of the Ubl and USP domains in full-length USP14.
  • To understand how USP14's conformation facilitates proteasome interaction.

Main Methods:

  • Nuclear magnetic resonance (NMR) spectroscopy was used to study the Ubl domain and full-length USP14.
  • Small-angle X-ray scattering (SAXS) and molecular modeling were employed to visualize the protein ensemble.

Main Results:

  • Transient interdomain interactions between the Ubl and USP domains were identified in USP14.
  • These interactions pre-dispose USP14's conformational ensemble for binding to the proteasome.

Conclusions:

  • The findings elucidate the mechanism by which USP14 interacts with the proteasome.
  • Understanding these interactions can inform the design of novel USP14 inhibitors for therapeutic applications.