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The E3 ligase TRIM13 restrains LPS-induced inflammation by reducing STIM1 abundance and the IRE1α-dependent unfolded protein response
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DOI：10.1126/scisignal.aeb2470.png)
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Abstract
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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
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