USP31

Last update 23 Jan 2025

Basic Info

Synonyms

Deubiquitinating enzyme 31, KIAA1203, Ubiquitin carboxyl-terminal hydrolase 31

+ [4]

Introduction

May recognize and hydrolyze the peptide bond at the C-terminal Gly of ubiquitin. Involved in the processing of poly-ubiquitin precursors as well as that of ubiquitinated proteins (By similarity).

100 Clinical Results associated with USP31

100 Translational Medicine associated with USP31

0 Patents (Medical) associated with USP31

191

Literatures (Medical) associated with USP31

01 Jan 2025·Biochemical and Biophysical Research Communications

USP21 stabilizes immune checkpoint of CD276 and serves as an immunological and tumor prognostic biomarker

Article

Author: Yu, Zhu ; Dong, Chengyuan ; Ge, Xin ; Yang, Yanrong ; Zheng, Zening

Ubiquitin-specific protease 21 (USP21) belongs to the ubiquitin-specific protease family and is a member of the deubiquitinating enzyme (DUB) family. Previous research has shown that USP21 promotes cancer initiation and progression. However, there have been few pan-cancer analysis on USP21. We analyzed the expression levels of USP21 mRNA and protein in various human tumor tissues using several public databases such as The Cancer Genome Atlas (TCGA), Genotype Tissue Expression (GTEx), and Human Protein Atlas (HPA). Kaplan-Meier survival analyses were utilized to test the effect of USP21 on overall survival (OS) and progression-free interval (PFS) of these tumor patients. Our study demonstrated that USP21 was differentially expressed between normal and malignant tissues, conferring a notable value in evaluation of prognosis and diagnosis. In addition, enrichment and correlation analyses linking USP21 with immune features such as immune-cell-infiltration rate and immune-checkpoint-gene expression indicated that USP21 is an applicable immunotherapeutic marker for liver cancer. To further elucidate the role of USP21, we downregulated its expression in hepatocellular carcinoma cells and identified a remarkable decrease in expression of the immune checkpoint CD276, which contributes to the immune escape of tumor cells by suppressing the immune system. Together, our results indicated a promising potential of USP21 for future tumor prevention.

01 Jan 2025·Shock

USP31 PROMOTES THE INFLAMMATORY RESPONSE OF HUMAN LUNG ORGANOIDS TO LIPOPOLYSACCHARIDE TREATMENT

Article

Author: Huang, Peng ; Xiao, Wenbiao ; Wang, Ying ; Lin, Bingwen ; Lin, Jiandong ; Xiao, Xiongjian

ABSTRACTBackground: Acute lung injury (ALI) is a severe condition characterized by a high mortality rate, driven by an uncontrolled inflammatory response. Emerging evidence has underscored the crucial role of the ubiquitin system in ALI. However, because of their vast number, the specific functions of individual ubiquitination regulators remain unclear. Materials and methods: In this study, we established human lung organoids (HLOs) derived from human embryonic stem cells and subjected them to lipopolysaccharide (LPS) treatment to induce an inflammatory response, mimicking ALI. Subsequently, we detected the expression of inflammatory cytokines, including tumor necrosis factor alpha (TNF-α), interleukin 6, interleukin 18 (IL-18), and interleukin-1β (IL-1β), by quantitative polymerase chain reaction experiments. We also detected changes in the mRNA expression of several USPs before and after HLOs treatment and thus screened for USPs that had significant changes in HLOs after LPS stimulation. After screening for USP, we silenced the USP in HLOs and then subjected them to LPS treatment, and TNF-α, IL-6, IL-18, and IL-1β expressions were detected using quantitative polymerase chain reaction assays. Meanwhile, western blot was used to detect changes in NOD-, LRR-, and pyrin domain-containing 3 (NLRP3) and apoptosis-associated Speck-like protein containing a CARD (ASC) protein level in HLOs. Results: Through screening the expression of 40 ubiquitin-specific proteases (USPs), which are responsible for removing ubiquitination, we identified several USPs that exhibited differential expression in LPS-treated HLOs compared to untreated HLOs. Notably, USP31 emerged as the most significantly upregulated USP, and the knockdown of USP31 markedly attenuated the inflammatory response of HLOs to LPS treatment. Conclusions: USP31 may play a facilitating role in the inflammatory response during ALI.

01 Dec 2024·Cellular and Molecular Life Sciences

USP28 promotes tumorigenesis and cisplatin resistance by deubiquitinating MAST1 protein in cancer cells

Article

Author: Kim, Kye-Seong ; Hong, Seok-Ho ; Jo, Won-Jun ; Colaco, Jencia Carminha ; Suresh, Bharathi ; Ko, Nare ; Oh, Seung Jun ; Ramakrishna, Suresh ; Woo, Sang Hyeon ; Singh, Vijai ; Tyagi, Apoorvi ; Karapurkar, Janardhan Keshav

AbstractCisplatin is a chemotherapy drug that causes a plethora of DNA lesions and inhibits DNA transcription and replication, resulting in the induction of apoptosis in cancer cells. However, over time, patients develop resistance to cisplatin due to repeated treatment and thus the treatment efficacy is limited. Therefore, identifying an alternative therapeutic strategy combining cisplatin treatment along with targeting factors that drive cisplatin resistance is needed. CRISPR/Cas9 system-based genome-wide screening for the deubiquitinating enzyme (DUB) subfamily identified USP28 as a potential DUB that governs cisplatin resistance. USP28 regulates the protein level of microtubule-associated serine/threonine kinase 1 (MAST1), a common kinase whose expression is elevated in several cisplatin-resistant cancer cells. The expression level and protein turnover of MAST1 is a major factor driving cisplatin resistance in many cancer types. Here we report that the USP28 interacts and extends the half-life of MAST1 protein by its deubiquitinating activity. The expression pattern of USP28 and MAST1 showed a positive correlation across a panel of tested cancer cell lines and human clinical tissues. Additionally, CRISPR/Cas9-mediated gene knockout of USP28 in A549 and NCI-H1299 cells blocked MAST1-driven cisplatin resistance, resulting in suppressed cell proliferation, colony formation ability, migration and invasion in vitro. Finally, loss of USP28 destabilized MAST1 protein and attenuated tumor growth by sensitizing cells to cisplatin treatment in mouse xenograft model. We envision that targeting the USP28-MAST1 axis along with cisplatin treatment might be an alternative therapeutic strategy to overcome cisplatin resistance in cancer patients.

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