Palmitoylation Induced Activation of SMAD3 Exacerbates Colitis by Promoting Tissue-resident Memory T Cells Differentiation

Tissue-resident memory T cells (TRM cells) have been shown to play an instrumental role in driving the onset and relapse of inflammatory bowel diseases (IBD). However, the underlying mechanism of TRM cells differentiation and its regulation in intestines remain to be unveiled. Mothers against decapentaplegic homolog 3 (SMAD3) is translocated from nucleus to membrane and activated in response to transforming growth factor beta (TGF-β), which is a key cytokine in the process of TRM cells polarization. Cysteine palmitoylation (S-palmitoylation) is a post-translational modification catalyzed by the DHHC family, regulating protein membrane associations. Genes associated with the classic SMAD3 signaling pathway, along with most genes in the DHHC family, were upregulated in TRM cells. Our study demonstrated that SMAD3 underwent reversible S-palmitoylation on Cys31 by DHHC6, leading to SMAD3 endomembrane recruitment and its subsequent colocalization with TGF-β receptor I (TGF-βRI) under TRM polarization conditions. The membrane recruitment of SMAD3 activated SMAD3 and subsequently upregulated the expression of its target genes, inducing the differentiation of TRM cells. In contrast, perturbation in DHHC6-induced palmitoylation with MYD-4 inhibited TRM cells differentiation and alleviated colitis in IBD model mice. Our work provides an example how the immune responses are regulated through the S-palmitoylation-dependent SMAD3 signaling in TRM cells differentiation and reveals protein S-palmitoylation as a potential target in IBD treatment, which could be of greater application considering the wide involvement of protein S-palmitoylation in the signal transduction in mammalian cells. The differentiation of TRM cells is promoted through TGF-β/SMAD3 pathway. The palmitoylation of SMAD3 on Cys31 by DHHC6 drives the membrane localization, the phosphorylation and the activation of SMAD3 under TRM polarization conditions. Inhibiting the differentiation of TRM cells by blocking palmitoylation of SMAD3 ameliorates colitis.

Authors

Institutions

Publication Details

Journal
Inflammation
Published
2026-03-04
DOI
https://doi.org/10.1007/s10753-026-02466-x
Primary Topic
Immune responses and vaccinations
Type
article
Field-Weighted Citation Impact
0.00
Controls
|||
ALL TIME
JAN
FEB
MAR
APR
MAY
JUN
JUL
AUG
SEP
OCT
article

Palmitoylation Induced Activation of SMAD3 Exacerbates Colitis by Promoting Tissue-resident Memory T Cells Differentiation

Yuejie Xu, Zhenguo Zhao, Mingming Zhang, Xiaoping Zou et al.
Inflammation
Immune responses and vaccinations
article

Palmitoylation Induced Activation of SMAD3 Exacerbates Colitis by Promoting Tissue-resident Memory T Cells Differentiation

Yuejie Xu, Zhenguo Zhao, Mingming Zhang, Xiaoping Zou, Ping Jiang, Jing Sun, Yu Zhao, Jian Tang, Guifang Xu, Qian Zhou, Shafi Ullah, Siqi Ji, Dan Su
article en

Abstract

Tissue-resident memory T cells (TRM cells) have been shown to play an instrumental role in driving the onset and relapse of inflammatory bowel diseases (IBD). However, the underlying mechanism of TRM cells differentiation and its regulation in intestines remain to be unveiled. Mothers against decapentaplegic homolog 3 (SMAD3) is translocated from nucleus to membrane and activated in response to transforming growth factor beta (TGF-β), which is a key cytokine in the process of TRM cells polarization. Cysteine palmitoylation (S-palmitoylation) is a post-translational modification catalyzed by the DHHC family, regulating protein membrane associations. Genes associated with the classic SMAD3 signaling pathway, along with most genes in the DHHC family, were upregulated in TRM cells. Our study demonstrated that SMAD3 underwent reversible S-palmitoylation on Cys31 by DHHC6, leading to SMAD3 endomembrane recruitment and its subsequent colocalization with TGF-β receptor I (TGF-βRI) under TRM polarization conditions. The membrane recruitment of SMAD3 activated SMAD3 and subsequently upregulated the expression of its target genes, inducing the differentiation of TRM cells. In contrast, perturbation in DHHC6-induced palmitoylation with MYD-4 inhibited TRM cells differentiation and alleviated colitis in IBD model mice. Our work provides an example how the immune responses are regulated through the S-palmitoylation-dependent SMAD3 signaling in TRM cells differentiation and reveals protein S-palmitoylation as a potential target in IBD treatment, which could be of greater application considering the wide involvement of protein S-palmitoylation in the signal transduction in mammalian cells. The differentiation of TRM cells is promoted through TGF-β/SMAD3 pathway. The palmitoylation of SMAD3 on Cys31 by DHHC6 drives the membrane localization, the phosphorylation and the activation of SMAD3 under TRM polarization conditions. Inhibiting the differentiation of TRM cells by blocking palmitoylation of SMAD3 ameliorates colitis.

Inflammation
Sun Yat-sen University (CN), Anhui Medical University (CN), Fujifilm (Japan) (JP), University of Chicago (US), Fudan University Shanghai Cancer Center (CN), Sixth Affiliated Hospital of Sun Yat-sen University (CN), Jiangyin People's Hospital (CN), Nanjing Drum Tower Hospital (CN), Suning (China) (CN), Zhongshan Hospital (CN), First Affiliated Hospital of Anhui Medical University (CN), State Key Laboratory of Oncogene and Related Genes (CN), Wuxi People's Hospital (CN), National Supercomputing Center in Wuxi (CN), Tang Hospital (CN)
Zero hunger
Openalex Percentile: Top 34%
Immune responses and vaccinations
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.