E3 ubiquitin ligases for MHC molecules.
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.
Ishido
Satoshi
S
RIKEN Research Center for Allergy and Immunology, Suehiro-cho, Tsurumi-ku, Yokohama, Kanagawa, Japan. ishido@rcai.riken.jp
Goto
Eiji
E
Matsuki
Yohei
Y
Ohmura-Hoshino
Mari
M
D000818:Animals; D003602:Cytotoxicity, Immunologic; D005786:Gene Expression Regulation / Q000276:immunology; D006649:Histocompatibility Antigens / Q000235:genetics / Q000276:immunology / Q000378:metabolism*; D006801:Humans; D007111:Immunity, Cellular; D021381:Protein Transport; D054829:RING Finger Domains / Q000276:immunology; D044767:Ubiquitin-Protein Ligases / Q000276:immunology* / Q000378:metabolism; D054875:Ubiquitination / Q000276:immunology; D014764:Viral Proteins / Q000276:immunology* / Q000378:metabolism; D014774:Virulence; D014777:Virus Diseases / Q000276:immunology*; D014780:Viruses / Q000201:enzymology / Q000276:immunology / Q000472:pathogenicity
D006649:Histocompatibility Antigens; D014764:Viral Proteins; C528121:MARCHF1 protein, human; D044767:Ubiquitin-Protein Ligases