TRIM2

Last update 08 May 2025

Basic Info

Synonyms

CMT2R, E3 ubiquitin-protein ligase TRIM2, KIAA0517

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Introduction

UBE2D1-dependent E3 ubiquitin-protein ligase that mediates the ubiquitination of NEFL and of phosphorylated BCL2L11. Plays a neuroprotective function. May play a role in neuronal rapid ischemic tolerance. Plays a role in antiviral immunity and limits New World arenavirus infection independently of its ubiquitin ligase activity (PubMed:24068738).

100 Clinical Results associated with TRIM2

100 Translational Medicine associated with TRIM2

0 Patents (Medical) associated with TRIM2

Literatures (Medical) associated with TRIM2

01 Apr 2025·International Journal of Biological Macromolecules

Corrigendum to “Genome-scale CRISPR screen identifies TRIM2 and SLC35A1 associated with porcine epidemic diarrhoea virus infection” [Int. J. Biol. Macromol. 250 (2023) 125962]

Author: Sun, Limeng ; Yin, Dongdong ; Wang, Jieru ; Liu, Hailong ; Zeng, Xiaoyu ; Yang, Yuqing ; Pan, Xiaocheng ; Zhao, Shuhong ; Li, Sheng ; Peng, Guiqing ; Tan, Yubei ; Ruan, Jinxue ; Wang, Chonglong ; Xie, Shengsong ; Wang, Zichang ; Shen, Xuehuai ; Yin, Lei ; Li, Xinyun ; Dai, Yin ; Guo, Zishi ; Liu, Xiangdong

01 Jan 2025·The FEBS Journal

TRIM2: a double‐edged sword preventing apoptosis

Article

Author: Hollemann, Thomas

TRIM2 belongs to the TRIM‐NHL class of ubiquitin E3‐ligases and inhibits apoptosis by a dual function. Liao et al. reported in the recent issue that under glutamine deprivation, TRIM2 transcription is activated by ATF4 to increase the uptake of long fatty acids into mitochondria. Here, TRIM2 acts as a direct activator of CPT1 independent of its E3 ubiquitin ligase activity and prevents apoptosis otherwise triggered by starvation. On the contrary, TRIM E3‐ubiquitin ligase has been described to ubiquitinate and thus target proapoptotic BIM for its degradation in the proteasome. Thus, TRIM2 inhibits apoptosis classically via its ligase activity but also independent of this stimulating energy metabolism.

01 Jan 2025·The FEBS Journal

TRIM2 promotes metabolic adaptation to glutamine deprivation via enhancement of CPT1A activity

Article

Author: Wang, Zhongyu ; Mei, Yide ; Liao, Kaimin ; Liu, Kaiyue ; Zhao, Kailiang

Cancer cells undergo metabolic adaptation to promote their survival and growth under energy stress conditions, yet the underlying mechanisms remain largely unclear. Here, we report that tripartite motif‐containing protein 2 (TRIM2) is upregulated in response to glutamine deprivation by the transcription factor cyclic AMP‐dependent transcription factor (ATF4). TRIM2 is shown to specifically interact with carnitine O‐palmitoyltransferase 1 (CPT1A), a rate‐limiting enzyme of fatty acid oxidation. Via this interaction, TRIM2 enhances the enzymatic activity of CPT1A, thereby regulating intracellular lipid levels and protecting cells from glutamine deprivation‐induced apoptosis. Furthermore, TRIM2 is able to promote both in vitro cell proliferation and in vivo xenograft tumor growth via CPT1A. Together, these findings establish TRIM2 as an important regulator of the metabolic adaptation of cancer cells to glutamine deprivation and implicate TRIM2 as a potential therapeutic target for cancer.

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TRIM2

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