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Review
. 2023 Oct 5:14:1210330.
doi: 10.3389/fendo.2023.1210330. eCollection 2023.

The role of TRIM family in metabolic associated fatty liver disease

Jingyue Zhang  1 , Yingming Zhang  1 , Ze Ren  1 , Dongmei Yan  2 , Guiying Li  1
Affiliations
Review

The role of TRIM family in metabolic associated fatty liver disease

Jingyue Zhang et al. Front Endocrinol (Lausanne). .

Abstract

Metabolic associated fatty liver disease (MAFLD) ranks among the most prevalent chronic liver conditions globally. At present, the mechanism of MAFLD has not been fully elucidated. Tripartite motif (TRIM) protein is a kind of protein with E3 ubiquitin ligase activity, which participates in highly diversified cell activities and processes. It not only plays an important role in innate immunity, but also participates in liver steatosis, insulin resistance and other processes. In this review, we focused on the role of TRIM family in metabolic associated fatty liver disease. We also introduced the structure and functions of TRIM proteins. We summarized the TRIM family's regulation involved in the occurrence and development of metabolic associated fatty liver disease, as well as insulin resistance. We deeply discussed the potential of TRIM proteins as targets for the treatment of metabolic associated fatty liver disease.

Keywords: TRIM family; insulin resistance; metabolic associated fatty liver disease; metabolism; ubiquitination.

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Conflict of interest statement

The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest.

Figures

Figure 1
Figure 1
Members and protein structure of TRIM family. Proteins of TRIM family contain more than 80 members. This includes a RING-finger domain, one or two B-box zinc-finger domains, and a coiled-coil domain, collectively forming the RBCC domain specific to the TRIM family. Given the significant variability in the C-terminal domain, TRIM proteins possessing a RING domain can be categorized into 11 subgroups, ranging from C-I to C-XI. R, RING domain; B, B-box domain; CC, coiled-coil domain; COS, Cos-box domain; ACID, Acid domain; FN3, Type III fibronectin repeat sequence; PRY, PRY domain; SPRY, SPRY domain; ARF, ADP-ribosylation factor family domain; BROMO, Bromo domain; FIL, Silk protein immunoglobulin domain; MATH, Meprin and TRAF homologous domains; NHL, NCL1, HT2A and LIN41 domains; TM, Transmembrane domain.
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The authors declare financial support was received for the research, authorship, and/or publication of this article. This work was supported by the National Natural Science Foundation of China (Grant No. 82270650), the Natural Science Foundation of Jilin Province, China (Grant No. 20210101003JC) and Graduate Innovation Fund of Jilin University.

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