E3 ubiquitin ligases for MHC molecules

Curr Opin Immunol. 2009 Feb;21(1):78-83. doi: 10.1016/j.coi.2009.01.002. Epub 2009 Feb 7.

Abstract

Recently, novel E3 ubiquitin ligases that target MHC molecules for lysosomal degradation have been discovered by several groups. All these E3s are membrane-bound and possess a variant type RING domain, termed the RING-CH or RING variant (RINGv) domain. They belong to a new E3 family designated Modulator of Immune Recognition (MIR), based on the name of the first identified family members. The discovery of the MIR family has provided fresh insight into viral pathogenesis and immune regulation.

Publication types

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

MeSH terms

  • Animals
  • Cytotoxicity, Immunologic
  • Gene Expression Regulation / immunology
  • Histocompatibility Antigens / genetics
  • Histocompatibility Antigens / immunology
  • Histocompatibility Antigens / metabolism*
  • Humans
  • Immunity, Cellular*
  • Protein Transport
  • RING Finger Domains / immunology
  • Ubiquitin-Protein Ligases / immunology*
  • Ubiquitin-Protein Ligases / metabolism
  • Ubiquitination / immunology
  • Viral Proteins / immunology*
  • Viral Proteins / metabolism
  • Virulence
  • Virus Diseases / immunology*
  • Viruses / enzymology
  • Viruses / immunology
  • Viruses / pathogenicity

Substances

  • Histocompatibility Antigens
  • Viral Proteins
  • MARCHF1 protein, human
  • Ubiquitin-Protein Ligases