title: TRIM proteins as RING finger E3 ubiquitin ligases.
abstract: The tripartite motif(TRIM) proteins harboring the RING finger, B-box and coiled-coil (RBCC) domain motifs form a large protein family. The members of this family are involved in various biological processes, including growth, differentiation, apoptosis and transcription and also in diseases and oncogenesis. Recent studies have revealed that TRIM proteins play key roles in innate antiviral immunity. An accumulating body of evidence has demonstrated that some TRIM proteins function as E3 ubiquitin ligases in specific ubiquitin-mediated protein degradation pathways; however, the precise mechanisms underlying this function have not been fully elucidated. In this chapter, we focus on the TRIM family of proteins specially with regard to E3 ligase.
authors: Division of Gene Regulation and Signal Transduction, Research Centerfor Genomic Medicine, Saitama Medical University, Saitama, Japan.
authors: Kazuhiro
authors: K
authors: Ikeda
authors: Satoshi
authors: S
authors: Inoue
mesh_terms: D020816:Amino Acid Motifs; D000818:Animals; D006801:Humans; D008954:Models, Biological; D054829:RING Finger Domains; D025801:Ubiquitin / Q000378:metabolism; D044767:Ubiquitin-Protein Ligases / Q000737:chemistry* / Q000378:metabolism*; D054875:Ubiquitination
chemical_list: D025801:Ubiquitin; D044767:Ubiquitin-Protein Ligases