Abstract
The tripartite motif (TRIM) protein family is attracting increasing interest in oncology. As a protein family based on structure rather than function, a plethora of biological activities are described for TRIM proteins, which are implicated in multiple diseases including cancer. With hormone-driven cancers being among the leading causes of cancer-related death, TRIM proteins have been described to portrait tumor suppressive or oncogenic activities in these tumor types. This review describes the biological impact of TRIM proteins in relation to hormone receptor biology, as well as hormone-independent mechanisms that contribute to tumor cell biology in prostate, breast, ovarian and endometrial cancer. Furthermore, we point out common functions of TRIM proteins throughout the group of hormone-driven cancers. An improved understanding of the biological impact of TRIM proteins in cancer may pave the way for improved prognostication and novel therapeutics, ultimately improving cancer care for patients with hormone-driven cancers.
Highlights
The tripartite motif (TRIM) protein family represents a class of ubiquitously expressed proteins that have different roles in many cellular mechanisms and molecular pathways [1].The tripartite structure is exclusive to metazoans and has been maintained with few changes throughout evolution
Whilst only a few TRIM genes are present in invertebrates, a large expansion occurred with the evolution of vertebrates and especially in mammals, with 60 to 70 TRIM genes in mouse, rat, dog, cat and cow [2,3]
This study showed that TRIM28 knockdown reduced overall androgen receptor (AR)-DNA binding whereas TRIM24 knockdown shifted the AR cistrome to different sites [54]
Summary
The tripartite motif (TRIM) protein family represents a class of ubiquitously expressed proteins that have different roles in many cellular mechanisms and molecular pathways [1]. The tripartite structure is exclusive to metazoans and has been maintained with few changes throughout evolution. That encode proteins that share a similar structure referred to as the RBCC motif. This conserved structure consists of an N-terminal RING (Really Interesting New Gene) domain, adjacent to either one or two cysteine/histidine-rich motifs known as B-boxes C-terminus and in their overall domain structure. Most TRIM proteins have been defined as E3s based on the presence of the RING domain [8], which is responsible for the recruitment of E2 enzymes carrying ubiquitin [9]. Aided by the B boxes to enhance target recognition, the CC region is necessary for the interaction with TRIM family members and other proteins. Specificity for substrate recruitment and scaffold and can have enzymatic activity or chromatin binding capacity [14]
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