ArticleProtein science : a publication of the Protein Society2019
Structural and functional study of FK domain of Fstl1.
Article in Protein science : a publication of the Protein Society, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 26 citations in OpenAlex.
- FSTL1 promotes M2 polarization of macrophages via the DIP2A-Smad2/3 Axis in gastric cancer.Journal of translational medicine · 2026Article
- FSTL1 accelerates nucleus pulposus-derived mesenchymal stem cell apoptosis in intervertebral disc degeneration by activating TGF-β-mediated Smad2/3 phosphorylation.Journal of translational medicine · 2025Article
- FSTL1 and TLR4 interact with PEDV structural proteins to promote virus adsorption to host cells.Journal of virology · 2025Article
- Follistatin like-1 (Adipocyte · 2024Article
- FSTL1 Accelerates Nucleus Pulposus Cell Senescence and Intervertebral Disc Degeneration Through TLR4/NF-κB Pathway.Inflammation · 2024Article
- Key Proteins for Regeneration inScientifica · 2024Article
- Role of follistatin-like protein 1 in liver diseases.Experimental biology and medicine (Maywood, N.J.) · 2023Review
- Article
- The matricellular protein SPARC induces inflammatory interferon-response in macrophages during aging.Immunity · 2022Article
- The Expression of Follistatin-like 1 Protein Is Associated with the Activation of the EMT Program in Sjögren's Syndrome.Journal of clinical medicine · 2022Article
- Follistatin-like 1 promotes proliferation of matured human hypoxic iPSC-cardiomyocytes and is secreted by cardiac fibroblasts.Molecular therapy. Methods & clinical development · 2022Article
- Follistatin-Like Proteins: Structure, Functions and Biomedical Importance.Biomedicines · 2021Review
- Article
- Structural and functional study of FK domain of Fstl1.Protein science : a publication of the Protein Society · 2019Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Fstl1 is a TGF-β superfamily binding protein which involved in many pathological processes. The function of Fstl1 has been widely elucidated, but its structural characterization has not been explored. Here we solved the high-resolution crystal structure of FK domain of murine Fstl1, analyzed its unique characteristics, and investigated its contribution to the function of full-length Fstl1. We found that Fstl1-FK forms a stable dimer in both solution and crystal, which suggest that this protein may function as a dimer during its interaction with TGF-β, a molecule known to form dimer during activation process. We also found this FK domain is indispensable for the proper function of Fstl1 during the transduction of TGF-β signaling. These observations provide important insights into the understanding of Fstl1 and may facilitate the exploration of this molecule in clinical study.
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