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.
Members of the tripartite motif (TRIM) protein family are found in all multicellular eukaryotes and function in a wide range of cellular processes such as cell cycle regulation, differentiation, development, oncogenesis and viral response. Over the past few years, several TRIM proteins have...
The TRIM/RBCC proteins belong to a family whom members are involved in a variety of cellular processes such as apoptosis and cell cycle regulation. These proteins are defined by the presence of a tripartite motif composed of three zinc‑binding domains, a RING finger, one or two B‑box...
MuRFs, brief for muscle specific RING finger proteins, correspond to a subfamily of the TRIM/RBCC protein family. Here, we review recent progress on the structural biology of MuRF1, the MuRF family member being most clearly associated with muscle diseases. The emerging understanding of the...
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...
Tripartite motif (TRIM) proteins are defined by their possession of a RING, B‑box and predicted coiled coil (RBCC) domain. The coiled‑coil region facilitates the oligomerisation of TRIMs and contributes to the formation of high molecular weight complexes that show interesting subcellular...
The TRIM family comprises proteins characterized by the presence of the tripartite motif that is composed of a RING domain, one or two B‑box domains and a Coiled‑coil region. These proteins are implicated in a plethora of cellular processes such as apoptosis, cell cycle regulation,...
Many TRIM proteins are up‑regulated by interferons, suggesting that they might be involved in the innate immune response against viruses. Indeed, some members of the family have been shown to be either regulators of the interferon pathways or to be directly involved in the restriction of...
TRIM proteins play important roles in several patho‑physiological processes. Their common activity within the ubiquitylation pathway makes them amenable to a number of diverse biological roles. Many of the TRIM genes are highly and sometimes specifically expressed during embryogenesis, it is...
TRIM proteins are multidomain proteins that typically assemble into large molecular complexes, the composition of which likely explains the diverse functions that have been attributed to this group of proteins. Accumulating data on the roles of many TRIM proteins supports the notion that those...
Some members of the tripartite motif (TRIM/RBCC) protein family are thought to be important regulators of carcinogenesis. This is not surprising as the TRIM proteins are involved in several biological processes, such as cell growth, development and cellular differentiation and alteration of...