ASB3 expression aggravates inflammatory bowel disease by targeting TRAF6 protein stability and affecting the intestinal microbiota

Ubiquitination is a key process that controls protein stability. We determined the ubiquitination of TRAF6 by ASB3 in intestinal epithelial cells during colonic inflammation. Inflammatory bowel disease patients exhibit upregulated ASB3 expression at focal sites, supporting the involvement of degradation of TRAF6, which promotes TLR-Myd88/TRIF-independent NF-κB aberrant activation and intestinal microbiota imbalance. Sustained inflammatory signaling in intestinal epithelial cells and dysregulated protective probiotic immune responses mediated by ASB3 collectively contribute to the exacerbation of inflammatory bowel disease. These findings provide insights into the pathogenesis of inflammatory bowel disease and suggest a novel mechanism by which ASB3 increases the risk of colitis. Our results suggest that future inhibition of ASB3 in intestinal epithelial cells may be a novel clinical strategy.

Authors

Institutions

Publication Details

Journal
mBio
Published
2024-08-20
DOI
https://doi.org/10.1128/mbio.02043-24
Citations
5
Primary Topic
NF-κB Signaling Pathways
Type
article
Field-Weighted Citation Impact
1.43

Funders

Controls
|||
ALL TIME
JAN
FEB
MAR
APR
MAY
JUN
JUL
AUG
SEP
OCT
article

ASB3 expression aggravates inflammatory bowel disease by targeting TRAF6 protein stability and affecting the intestinal microbiota

Yiyuan Lu, Yanlong Jiang, Tianxu Pan, Dongqin Yang et al.
5 citations
mBio
NF-κB Signaling Pathways
1.43
article

ASB3 expression aggravates inflammatory bowel disease by targeting TRAF6 protein stability and affecting the intestinal microbiota

Yiyuan Lu, Yanlong Jiang, Tianxu Pan, Dongqin Yang, Xin Cao, Mingyang Cheng, Haibin Huang, Yan Zeng, Yu Sun, Guilian Yang, Chunwei Shi, Wentao Yang, Nan Wang, Jianzhong Wang, Chunfeng Wang, Junhong Wang, Xiaoxu Li, Wenhui Zhao, Bin Xu, Xiaomei Song
article en
5 citations

Abstract

Ubiquitination is a key process that controls protein stability. We determined the ubiquitination of TRAF6 by ASB3 in intestinal epithelial cells during colonic inflammation. Inflammatory bowel disease patients exhibit upregulated ASB3 expression at focal sites, supporting the involvement of degradation of TRAF6, which promotes TLR-Myd88/TRIF-independent NF-κB aberrant activation and intestinal microbiota imbalance. Sustained inflammatory signaling in intestinal epithelial cells and dysregulated protective probiotic immune responses mediated by ASB3 collectively contribute to the exacerbation of inflammatory bowel disease. These findings provide insights into the pathogenesis of inflammatory bowel disease and suggest a novel mechanism by which ASB3 increases the risk of colitis. Our results suggest that future inhibition of ASB3 in intestinal epithelial cells may be a novel clinical strategy.

mBioVol. 15(9)
Tongji University (CN), Fudan University (CN), Jilin Agricultural University (CN), Huashan Hospital (CN), First People's Hospital of Chongqing (CN)
National Natural Science Foundation of China, Fudan University, Tongji University, Chinese Academy of Agricultural Sciences, Huashan Hospital, Lanzhou Veterinary Research Institute, Chinese Academy of Agricultural Sciences
Good health and well-being
Openalex Percentile: Top 18%
NF-κB Signaling Pathways
1.43
DOIOpen Access PDFOpenAlex
AI Navigator

Ask Laika to Summarize, Analyze, and Connect papers live on the map.

Summarize Papers & Methodologies

Extract key findings, datasets, and comparative methods across publications.

Benchmark Rankings & Visual Analytics

Rank top research institutions, authors, funders, topics, and journals by Field-Weighted Citation Impact (FWCI) and paper volume with instant charts.

Connect Distant Disciplines

Bridge topological clusters on the map to find hidden collaborative intersections.