The tripartite motif structure and function

Lucia Micale, Evelyne Chaignat, Carmela Fusco, Alexandre Reymond, Giuseppe Merla

Research output: Chapter in Book/Report/Conference proceedingChapter

Abstract

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 motifs, a coiled-coil region and a highly variable C-terminal region. Interestingly, the preserved order of the tripartite motif from the N-to the C-terminal end of the protein and the highly conserved overall architecture of this motif throughout evolution suggest that common biochemical functions may underline their assorted cellular roles. Here we present the structure and the proposed function of each TRIM domain including the highly variable C-terminal domain.

Original languageEnglish
Title of host publicationAdvances in Experimental Medicine and Biology
Pages11-25
Number of pages15
Volume770
DOIs
Publication statusPublished - 2012

Publication series

NameAdvances in Experimental Medicine and Biology
Volume770
ISSN (Print)00652598

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ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Medicine(all)

Cite this

Micale, L., Chaignat, E., Fusco, C., Reymond, A., & Merla, G. (2012). The tripartite motif structure and function. In Advances in Experimental Medicine and Biology (Vol. 770, pp. 11-25). (Advances in Experimental Medicine and Biology; Vol. 770). https://doi.org/10.1007/978-1-4614-5398-7_2