Ubiquitin signaling in immune responses

Cell Res. 2016 Apr;26(4):457-83. doi: 10.1038/cr.2016.40. Epub 2016 Mar 25.

Abstract

Ubiquitination has emerged as a crucial mechanism that regulates signal transduction in diverse biological processes, including different aspects of immune functions. Ubiquitination regulates pattern-recognition receptor signaling that mediates both innate immune responses and dendritic cell maturation required for initiation of adaptive immune responses. Ubiquitination also regulates the development, activation, and differentiation of T cells, thereby maintaining efficient adaptive immune responses to pathogens and immunological tolerance to self-tissues. Like phosphorylation, ubiquitination is a reversible reaction tightly controlled by the opposing actions of ubiquitin ligases and deubiquitinases. Deregulated ubiquitination events are associated with immunological disorders, including autoimmune and inflammatory diseases.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Dendritic Cells / physiology
  • Immune Tolerance
  • Immunity*
  • Inflammation / immunology
  • Mitogen-Activated Protein Kinases / metabolism
  • Receptors, Cell Surface / metabolism
  • Signal Transduction*
  • T-Lymphocytes / immunology
  • Ubiquitin / metabolism*
  • Ubiquitination*

Substances

  • Receptors, Cell Surface
  • Ubiquitin
  • Mitogen-Activated Protein Kinases