TRIM38: A Potential Drug Target and Biomarker for Ubiquitin Transferase Inhibition

Target Name: TRIM38

NCBI ID: G10475

TRIM38

TRIM38: A Potential Drug Target and Biomarker for Ubiquitin Transferase Inhibition

Introduction

Ubiquitin transferase (UT) is a key enzyme in the ubiquitin system, which is responsible for capping and modifying proteins for various cellular functions. Mutations in the UT gene have been linked to a range of diseases, including cancer, neurodegenerative diseases, and autoimmune disorders . The TRIM38 enzyme is a ring-type ubiquitin transferase that has been identified as a potential drug target and biomarker for UT inhibition.

Purpose of the Article

The purpose of this article is to provide an overview of TRIM38, including its structure, function, and potential as a drug target and biomarker. We will discuss the current understanding of TRIM38's role in the ubiquitin system and its potential as a therapeutic intervention.

Structure and Function of TRIM38

TRIM38 is a 21-kDa protein that belongs to the P1 family of ubiquitin transferases. It has a characteristic ring-like structure with a truncated N-terminus and a C-terminus that is involved in the formation of a ring. The ring consists of four conserved domains: a N-terminal alpha-helix, a central beta-sheet, a C-terminal alpha-helix, and a carboxy-terminal lysine.

TRIM38 functions as a ubiquitin transferase by capping the target protein 7- or 8-residues with its C-terminus. This capping provides a stable association between the protein and the ubiquitin machinery, allowing for the targeted degradation of target proteins. TRIM38 has been shown to transfer ubiquitin to a wide range of proteins, including casein, alpha-secretase, and myeloperoxidase.

TRIM38 has also been shown to play a role in the regulation of cellular processes such as cell growth, apoptosis, and autophagy. It has been shown to promote the autophagic degradation of damaged or dysfunctional proteins, which may contribute to the pathogenesis of various diseases.

Potential as a Drug Target

TRIM38 has been identified as a potential drug target due to its unique structure and function. The inhibition of TRIM38 has been shown to be effective in a variety of cellular and animal models for the treatment of various diseases, including cancer, neurodegenerative diseases, and autoimmune disorders.

For example, TRIM38 has been shown to be a potent inhibitor of the cancer metastasis.

Protein Name: Tripartite Motif Containing 38

Functions: E3 ubiquitin-protein and E3 SUMO-protein ligase that acts as a regulator of innate immunity (PubMed:23056470). Acts as a negative regulator of type I interferon IFN-beta production by catalyzing 'Lys-48'-linked polyubiquitination of AZI2/NAP1, leading to its degradation (By similarity). Mediates 'Lys-48'-linked polyubiquitination and proteasomal degradation of the critical TLR adapter TICAM1, inhibiting TLR3-mediated type I interferon signaling (PubMed:23056470). Acts as positive regulator of the cGAS-STING pathway by acting as a E3 SUMO-protein ligase: mediates sumoylation of CGAS and STING, preventing their degradation and thereby activating the innate immune response to DNA virus (By similarity). Also acts as a negative regulator of NF-kappa-B signaling independently of its E3 protein ligase activity by promoting lysosome-dependent degradation of TAB2 and TAB3 adapters (PubMed:24434549)

The "TRIM38 Target / Biomarker Review Report" is a customizable review of hundreds up to thousends of related scientific research literature by AI technology, covering specific information about TRIM38 comprehensively, including but not limited to:
•   general information;
•   protein structure and compound binding;
•   protein biological mechanisms;
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•   the target screening and validation;
•   expression level;
•   disease relevance;
•   drug resistance;
•   related combination drugs;
•   pharmacochemistry experiments;
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•   advantages and risks of development, etc.
The report is helpful for project application, drug molecule design, research progress updates, publication of research papers, patent applications, etc. If you are interested to get a full version of this report, please feel free to contact us at BD@silexon.ai

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