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TRIM/RBCC Proteins pp 27–37Cite as

Trim Proteins as Ring Finger E3 Ubiquitin Ligases

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Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 770))

Abstract

The tripartite motif (TRIM) proteins harboring the RING fmger, B-boxandcoiled-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.

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Authors and Affiliations

  1. Division of Gene Regulation and Signal Transduction, Research Center for Genomic Medicine, Saitama Medical University, Saitama, Japan

    Kazuhiro Ikeda & Satoshi Inoue

  2. Departments of Geriatric Medicine and Anti-Aging Medicine, Graduate School of Medicine, The University of Tokyo, Tokyo, Japan

    Satoshi Inoue

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  1. Kazuhiro Ikeda
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  2. Satoshi Inoue
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  1. Cluster in Biomedicine, CBM S.c.r.l., AREA Science Park, Trieste, Italy

    Germana Meroni Phd

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Ikeda, K., Inoue, S. (2012). Trim Proteins as Ring Finger E3 Ubiquitin Ligases. In: Meroni, G. (eds) TRIM/RBCC Proteins. Advances in Experimental Medicine and Biology, vol 770. Springer, New York, NY. https://doi.org/10.1007/978-1-4614-5398-7_3

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