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Updated: Dec 26, 2025

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UBB pseudogene 4 encodes functional ubiquitin variants.

Marie-Line Dubois1, Anna Meller1, Sondos Samandi2

  • 1Department of Immunology and Cell Biology, Sherbrooke, QC, Canada.

Nature Communications
|March 13, 2020
PubMed
Summary
This summary is machine-generated.

Pseudogenes, like UBBP4, can produce functional ubiquitin variants (UbKEKS) that modify proteins differently than standard ubiquitylation, impacting cell division and nuclear structure.

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Area of Science:

  • Molecular Biology
  • Genetics
  • Cell Biology

Background:

  • Pseudogenes are typically non-functional gene copies, but some express proteins.
  • Ubiquitin pseudogenes are abundant, yet their functions remain largely uncharacterized.
  • Previous studies have not fully explored the protein-level expression and signaling roles of ubiquitin pseudogenes.

Purpose of the Study:

  • To investigate the expression and functional potential of ubiquitin pseudogenes.
  • To identify novel protein products from pseudogenes and their targets.
  • To elucidate the cellular consequences of pseudogene-derived protein modifications.

Main Methods:

  • Re-analysis of public RNA-sequencing and proteomics datasets.
  • Quantitative proteomics to identify protein modifications.
  • Gene knockout experiments (UBBP4) to assess functional impact.
  • Analysis of cell division rates and protein localization.

Main Results:

  • Evidence for the expression of several ubiquitin pseudogenes, including UBBP4.
  • UBBP4 encodes a ubiquitin variant, UbKEKS, which modifies proteins like lamins.
  • UbKEKS conjugation has distinct functional consequences compared to canonical ubiquitylation.
  • UBBP4 knockout leads to impaired cell division and nucleolar accumulation of lamin A.

Conclusions:

  • A subset of pseudogenes, such as UBBP4, can produce functional ubiquitin variants.
  • These variants can alter protein function, impacting cellular processes.
  • The study suggests some reported ubiquitylation targets may be modified by pseudogene-derived variants, necessitating re-evaluation of protein modification pathways.