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Detection of Protein Ubiquitination
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Linear ubiquitination at a glance.

Maureen Spit1, Eva Rieser1, Henning Walczak2

  • 1Centre for Cell Death, Cancer, and Inflammation (CCCI), UCL Cancer Institute, University College London, 72 Huntley Street, London WC1E 6DD, UK.

Journal of Cell Science
|January 20, 2019
PubMed
Summary

The linear ubiquitin chain assembly complex (LUBAC) builds linear ubiquitin chains, essential for immune responses. Deubiquitinases controlling these chains add another layer to LUBAC-mediated signalling.

Keywords:
LUBACLinear ubiquitinTNF signalling

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Area of Science:

  • Molecular Biology
  • Cellular Biology
  • Immunology

Background:

  • Ubiquitination is a key post-translational modification regulating cellular processes.
  • Ubiquitin can form eight distinct inter-ubiquitin linkages.
  • Linear ubiquitin chains, formed via the M1 linkage, are critical for immune signalling.

Purpose of the Study:

  • To review the role of the linear ubiquitin chain assembly complex (LUBAC) in immune signalling.
  • To explore LUBAC's function in inflammation, gene activation, and cell death.
  • To highlight the impact of deubiquitinases (DUBs) on LUBAC-mediated signalling.

Main Methods:

  • Literature review of current knowledge on LUBAC and linear ubiquitination.
  • Focus on signalling pathways involving tumour necrosis factor (TNF).
  • Analysis of the roles of deubiquitinases (DUBs) in cleaving M1 linkages.

Main Results:

  • LUBAC is the sole E3 ligase known to synthesize linear ubiquitin chains.
  • Linear ubiquitin chains modulate innate and adaptive immunity, inflammation, and cell death.
  • DUBs that cleave M1 linkages provide regulatory control over LUBAC-dependent signalling.

Conclusions:

  • LUBAC and linear ubiquitination are central to immune signalling pathways.
  • Understanding LUBAC's role in TNF signalling is crucial for comprehending inflammation and cell fate.
  • DUBs offer a critical regulatory mechanism in LUBAC-mediated immune responses.