Emerging Roles and Research Tools of Atypical Ubiquitination

Proteomics. 2020 May;20(9):e1900100. doi: 10.1002/pmic.201900100. Epub 2020 Jan 30.

Abstract

Ubiquitination is a posttranslational modification characterized by the covalent attachment of ubiquitin molecules to protein substrates. The ubiquitination modification process is reversible, dynamic, and involved in the regulation of various biological processes, such as autophagy, inflammatory responses, and DNA damage responses. The forms of ubiquitin modification are very diverse, incorporating either a single ubiquitin molecule or a complicated ubiquitin polymer, and different types of ubiquitination usually elicit corresponding cellular responses. The development of research tools and strategies has afforded more detailed insight into atypical ubiquitin signaling pathways that were previously poorly understood. Here, an update on the understanding of atypical ubiquitin chain signaling pathways is provided and the recent development of representative research tools for ubiquitin systems is discussed. In addition, the future challenges in ubiquitin research are reflected on and summarized.

Keywords: DNA damage; TNF-α signaling; atypical ubiquitin chains; ubiquitin enrichment; ubiquitination.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Cell Death
  • Humans
  • Inflammation / metabolism
  • Lysine / metabolism
  • Proteasome Endopeptidase Complex
  • Protein Processing, Post-Translational
  • Proteins / analysis
  • Proteins / metabolism*
  • Proteomics / methods*
  • Signal Transduction
  • Ubiquitin / metabolism
  • Ubiquitination

Substances

  • Proteins
  • Ubiquitin
  • Proteasome Endopeptidase Complex
  • Lysine