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TitleNatural Asp-tRNA Synthetase Fragment Targets Myofibroblasts to Abrogate Tissue Fibrosis.
Journal, issue, pagesJ Biol Chem, Page 113586, Year 2026
Publish dateSep 30, 2026
AuthorsRyan A Adams / Ying-Ting Wang / Alison G Barber / Kristina Hamel / Andrew Imfeld / Luke Burman / Kaitlyn Rauch / Yeeting E Chong / Angelica Villanueva / Lauren Guy / Wayne Liu / Crystal Manzo / Sofia Klopp-Savino / Clara Polizzi / Jasmine Stamps / Max Pastenes / Honglei Tian / Chun Po Fung / Yingyi Zhang / Kwok Wa Hugo Ho / Bruno Sangiorgi / Blythe Dillingham / Tarsis F Brust / Kyle P Chiang / Zhenguo Wu / Zhiwen Xu / Christoph Burkart / Leslie A Nangle /
PubMed AbstractFibrosis remains a major global health challenge with limited therapies that only slow disease progression. While the aminoacyl-tRNA synthetase (aaRS) family is known to utilize evolutionarily ...Fibrosis remains a major global health challenge with limited therapies that only slow disease progression. While the aminoacyl-tRNA synthetase (aaRS) family is known to utilize evolutionarily appended domains as extracellular signaling molecules, their role in regulating the homeostasis of the fibrotic process is poorly defined. We identify a natural proteolytic fragment of aspartyl-tRNA synthetase (DARS), termed DARS-N1, that selectively triggers apoptosis in myofibroblasts by targeting latent-transforming growth factor beta binding protein 1 (LTBP-1) on the extracellular matrix (ECM). This active N-terminal fragment of DARS reduces focal adhesion kinase (FAK) activation in undifferentiated fibroblasts and myofibroblasts, while only myofibroblasts exhibit inadequate cell-matrix attachment leading to loss of anchorage-dependent survival and promotion of apoptosis. We utilized ATYR0101, a therapeutic form of DARS-N1 engineered for extended serum exposure, to demonstrate anti-fibrotic activity in lung (bleomycin). Spatial transcriptomics analysis showed that ATYR0101 activates a restorative program promoting the return to a healthy state. These findings highlight ATYR0101's potential as a transformative therapy for disrupting the process of chronic tissue fibrosis.
External linksJ Biol Chem / PubMed:42815638
MethodsEM (single particle)
Resolution4.96 Å
Structure data

67441

21aa

EMDB-67441, PDB-21aa:
Structure of Human Aspartate--tRNA ligase 3-154 with linker and FC : ATYR0101
Method: EM (single particle) / Resolution: 4.96 Å

Source
  • homo sapiens (human)
KeywordsAPOPTOSIS / Fibrosis / t-RNA synthase / Myofibroblast

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