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Updated: Aug 24, 2025

In Vitro Analysis of E3 Ubiquitin Ligase Function
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An expanded lexicon for the ubiquitin code.

Ivan Dikic1,2, Brenda A Schulman3

  • 1Institute of Biochemistry II, Faculty of Medicine, Goethe University, Frankfurt, Germany. dikic@biochem2.uni-frankfurt.de.

Nature Reviews. Molecular Cell Biology
|October 26, 2022
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Summary
This summary is machine-generated.

Pathogens manipulate the ubiquitin code through novel modifications and enzymatic pathways to promote infection. Understanding these processes offers new therapeutic strategies for cancer and infectious diseases.

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Profiling Ubiquitin and Ubiquitin-like Dependent Post-translational Modifications and Identification of Significant Alterations
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Area of Science:

  • Molecular Biology
  • Biochemistry
  • Immunology

Background:

  • The ubiquitin code, traditionally involving E1, E2, and E3 enzymes modifying lysine residues, has evolved to encompass more complex ubiquitylation processes.
  • Pathogens have developed sophisticated mechanisms to hijack and alter the host's ubiquitin system for their own benefit.

Purpose of the Study:

  • To review recently discovered endogenous mechanisms and pathways used by pathogens to manipulate the ubiquitin code.
  • To highlight unconventional ubiquitin modifications and the enzymes involved in their synthesis and reversal.
  • To discuss the structural basis of ubiquitin-protein interactions and their functional outcomes.

Main Methods:

  • Literature review of recent findings on ubiquitin modification and pathogen interactions.
  • Analysis of structural studies elucidating ubiquitin-binding domain recognition.
  • Discussion of enzymatic pathways involved in ubiquitylation and deubiquitylation.

Main Results:

  • Pathogens employ unconventional ubiquitin modifications, including ester linkages and phosphoribosyl bridges, to promote infection.
  • Enzymes like papain-like proteases of SARS-CoV and SARS-CoV-2 are key players in rewriting the ubiquitin code.
  • Multivalent interactions, rather than simple domain recognition, mediate ubiquitin's ultimate functions in protein degradation and transcription.

Conclusions:

  • Newly discovered ubiquitin code manipulation mechanisms by pathogens offer novel therapeutic targets.
  • Understanding these complex interactions is crucial for developing treatments for cancer and infectious diseases.