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The E3 ligase TRIM13 restrains LPS-induced inflammation by reducing STIM1 abundance and the IRE1α-dependent unfolded protein response

delete2026-07-14
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PRE
AI
Z
Zheng Li
X
Xuelian Li
Y
Yu Zhou
Q
Qian Fang
T
Tong Xia
J
Jiaying Huang
M
Mingjin Yang *
T
Taoyong Chen *
DOI：10.1126/scisignal.aeb2470delete
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Abstract

Abstract

En 中文
The E3 ubiquitin ligase TRIM13 is involved in ER-associated degradation (ERAD) of misfolded proteins. Li et al. found that TRIM13 limited inflammatory responses induced by the innate receptor TLR4. In mouse macrophages, TRIM13 targeted the ER-localized Ca2+ sensor STIM1 for degradation through the ERAD pathway, thereby reducing STIM1-dependent store-operated Ca2+ entry (SOCE). Increased SOCE in cells lacking TRIM13 enhanced TLR4-dependent inflammatory responses by inducing ER stress and the IRE1α branch of the ER stress response. In mice, myeloid-specific loss of TRIM13 exacerbated chemically induced colitis, which was partially rescued by IRE1α inhibition. Thus, TRIM13 curbs TLR4-dependent inflammation by supporting ER homeostasis. —Annalisa M. VanHook

Journal

Science Signaling cover
Science Signaling
IF:
6.6
Papers:
3.0K
Citations:
1.4W

Organization

C
chinese academy of medical sciences
Scholars:
575
Papers: 205
Citations: 0
N
naval medical university
Scholars:
4.7K
Papers: 1.4K
Citations: 175
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