Biological Functions and Therapeutic Potential of UBE2T in Human Cancer

The ubiquitin-proteasome system is a fundamental regulatory mechanism that governs protein stability and intracellular signaling in eukaryotic cells. This system relies on a coordinated cascade of enzymatic activities involving activating enzymes, conjugating enzymes, and ligases to assemble distinct ubiquitin signals. These signals are subsequently edited, removed, or interpreted by deubiquitinases and ubiquitin-binding proteins. While E3 ligases have traditionally been recognized as the primary determinants of substrate specificity in the ubiquitination process, recent studies have revealed that the dysregulation of E2 enzymes can also lead to significant pathological outcomes, including chromatin instability, immune dysregulation, metabolic dysfunction, and an elevated risk of cancer. Consequently, E2 enzymes have emerged as promising therapeutic targets for the treatment of various dis-eases. This review provides a comprehensive examination of the roles and mechanisms of the ubiquitin-conjugating enzyme E2T (UBE2T) in cancer initiation, progression, and therapy resistance, highlighting its potential as a compelling target for cancer therapeutics.

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Publication Details

Journal
Current Cancer Drug Targets
Published
2025-03-06
DOI
https://doi.org/10.2174/0115680096370867250211070948
Citations
2
Primary Topic
Ubiquitin and proteasome pathways
Type
article
Field-Weighted Citation Impact
1.61
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article

Biological Functions and Therapeutic Potential of UBE2T in Human Cancer

Yong Ma, Huinian Zhou, Xiangyan Jiang, Qichen He et al.
2 citations
Current Cancer Drug Targets
Ubiquitin and proteasome pathways
1.61
article

Biological Functions and Therapeutic Potential of UBE2T in Human Cancer

Yong Ma, Huinian Zhou, Xiangyan Jiang, Qichen He, Keshen Wang, Tao Wang, Zuoyi Jiao, Zeyuan Yu
article en
2 citations

Abstract

The ubiquitin-proteasome system is a fundamental regulatory mechanism that governs protein stability and intracellular signaling in eukaryotic cells. This system relies on a coordinated cascade of enzymatic activities involving activating enzymes, conjugating enzymes, and ligases to assemble distinct ubiquitin signals. These signals are subsequently edited, removed, or interpreted by deubiquitinases and ubiquitin-binding proteins. While E3 ligases have traditionally been recognized as the primary determinants of substrate specificity in the ubiquitination process, recent studies have revealed that the dysregulation of E2 enzymes can also lead to significant pathological outcomes, including chromatin instability, immune dysregulation, metabolic dysfunction, and an elevated risk of cancer. Consequently, E2 enzymes have emerged as promising therapeutic targets for the treatment of various dis-eases. This review provides a comprehensive examination of the roles and mechanisms of the ubiquitin-conjugating enzyme E2T (UBE2T) in cancer initiation, progression, and therapy resistance, highlighting its potential as a compelling target for cancer therapeutics.

Current Cancer Drug TargetsVol. 25
Lanzhou University Second Hospital (CN), Lanzhou University (CN)
Good health and well-being
Openalex Percentile: Top 19%
Ubiquitin and proteasome pathways
1.61
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Biological Functions and Therapeutic Potential of UBE2T in Human Cancer — Yong Ma, Huinian Zhou, et al. · Current Cancer Drug Targets (2025) | TGRS Research Map | TGRS