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Proteasome activity maintains cell-type-specific gene expression.

Xiuxiu Lu1, Vasty Osei-Amponsa1, Germán Michelis2

  • 1Protein Processing Section, Center for Structural Biology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Frederick, MD 21702, USA.

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|February 14, 2026
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Summary
This summary is machine-generated.

Proteasome activity is vital for maintaining cell identity by regulating gene expression. Losing ubiquitin-binding in hRpn10/PSMD4 disrupts this, leading to misexpressed proteins and altered cell types.

Keywords:
CP: molecular biologyOTUD5PSMD4Rpn10cell identitygene expressionproteasomeprotein degradationtissue specificitytranscriptional regulationubiquitin

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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • Regulated proteolysis via the ubiquitin-proteasome system is crucial for cellular functions like protein quality control, cell cycle, and DNA repair.
  • The ubiquitin-binding activity of proteasome substrate receptor hRpn10/PSMD4 is essential for substrate recognition and degradation.

Purpose of the Study:

  • To investigate the role of proteasome activity, specifically the ubiquitin-binding function of hRpn10/PSMD4, in maintaining cell identity.
  • To identify the molecular mechanisms by which proteasome dysfunction impacts cell-type-specific gene expression.

Main Methods:

  • Analysis of cells expressing truncated hRpn10 lacking ubiquitin interaction motifs (hRpn10VWA).
  • Proteomic and transcriptomic analysis to identify dysregulated proteins and gene expression patterns.
  • Investigating the role of OTUD5 accumulation in observed phenotypes.

Main Results:

  • Loss of hRpn10 ubiquitin-binding activity leads to significant protein dysregulation.
  • Altered proteins show overrepresentation of tissue-specific factors, indicating a loss of cell identity.
  • Accumulation of OTUD5, a deubiquitinase and transcriptional regulator, contributes to transcriptional dysregulation.

Conclusions:

  • Proteasome-dependent mechanisms are essential for safeguarding cell-type-specific gene expression programs.
  • Proteasome function extends beyond basic cellular maintenance to include the governance of cell identity.
  • Disruption of ubiquitin binding in hRpn10/PSMD4 compromises cell identity through transcriptional dysregulation.