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EMBO Journal

EMBO Journal

IF: 8.3
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ER-anchored CRTH2 antagonizes collagen biosynthesis and organ fibrosis via binding LARP6

Published:16 August 2021 DOI: 10.15252/embj.2020107403 PMID: 34223653
Shengkai Zuo,?Bei Wang,?Jiao Liu,?Deping Kong,?Hui Cui,?Yaonan Jia,?Chenyao Wang,?Xin Xu,?Guilin Chen,?Yuanyang Wang,?Linlin Yang,?Kai Zhang,?Ding Ai,?Jie Du,?Yujun Shen,?Ying Yu

Abstract

Excessive deposition of extracellular matrix, mainly collagen protein, is the hallmark of organ fibrosis. The molecular mechanisms regulating fibrotic protein biosynthesis are unclear. Here, we find that chemoattractant receptor homologous molecule expressed on TH2 cells (CRTH2), a plasma membrane receptor for prostaglandin D2, is trafficked to the endoplasmic reticulum (ER) membrane in fibroblasts in a caveolin-1-dependent manner. ER-anchored CRTH2 binds the collagen mRNA recognition motif of La ribonucleoprotein domain family member 6 (LARP6) and promotes the degradation of collagen mRNA in these cells. In line, CRTH2 deficiency increases collagen biosynthesis in fibroblasts and exacerbates injury-induced organ fibrosis in mice, which can be rescued by LARP6 depletion. Administration of CRTH2 N-terminal peptide reduces collagen production by binding to LARP6. Similar to CRTH2, bumetanide binds the LARP6 mRNA recognition motif, suppresses collagen biosynthesis, and alleviates bleomycin-triggered pulmonary fibrosis in?vivo. These findings reveal a novel anti-fibrotic function of CRTH2 in the ER membrane via the interaction with LARP6, which may represent a therapeutic target for fibrotic diseases.

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