ArticleScientific reports2021
Identification of the atypical cadherin FAT1 as a novel glypican-3 interacting protein in liver cancer cells.
Article in Scientific reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
29 citing papers in PubMed, 38 citations in OpenAlex.
- CSTF2-mediated 3'UTR shortening drives oncogenic activation of GPC3 in hepatocellular carcinoma.Oncogene · 2026Article
- Molecular Mechanisms of FAT Atypical Cadherin 1 (FAT1), the Hippo Pathway, and the Yes-Associated Protein (YAP) Signaling Pathways in Some Cancers.Asian Pacific journal of cancer prevention : APJCP · 2026Review
- Development of a model combining CEUS LI-RADS and clinical features for predicting glypican-3 expression in hepatocellular carcinoma.Abdominal radiology (New York) · 2025Article
- Review
- Targeting Glypican-3 for Liver Cancer Therapy: Clinical Applications and Detection Methods.Journal of clinical and translational hepatology · 2025Review
- Immune factors and their role in tumor aggressiveness in glioblastoma: Atypical cadherin FAT1 as a promising target for combating immune evasion.Cellular & molecular biology letters · 2025Review
- Recent advances in the role of atypical cadherin FAT1 in tumorigenesis (Review).Oncology letters · 2025Review
- Gallium-68 Labeled Positron Emission Computed Tomography Tracer Targeting Glypican-3 with High Contrast for Hepatocellular Carcinoma Imaging.ACS pharmacology & translational science · 2024Article
- GPC3-targeted CAR-M cells exhibit potent antitumor activity against hepatocellular carcinoma.Biochemistry and biophysics reports · 2024Article
- Article
- Pan-cancer analysis predict that FAT1 is a therapeutic target and immunotherapy biomarker for multiple cancer types including non-small cell lung cancer.Frontiers in immunology · 2024Article
- Review
- A Simple and Affordable Method to Create Nonsense Mutation Clones of p53 for Studying the Premature Termination Codon Readthrough Activity of PTC124.Biomedicines · 2023Article
- Comprehensive Genomic Profiling IdentifiesJournal of hepatocellular carcinoma · 2023Article
- PTC124 Rescues Nonsense Mutation of Two Tumor Suppressor GenesBiomedicines · 2022Article
- Review
- Expression, Prognostic Value, and Functional Mechanism of Polarity-Related Genes in Hepatocellular Carcinoma.International journal of molecular sciences · 2022Article
- Article
- The diverse functions of FAT1 in cancer progression: good, bad, or ugly?Journal of experimental & clinical cancer research : CR · 2022Review
- Excavating proteoglycan structure-function relationships: modern approaches to capture the interactions of ancient biomolecules.American journal of physiology. Cell physiology · 2022Review
Corrections and comments
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Authors and funding
10 authors at 4 institutions in 2 countries.
Funding
Abstract
Glypican-3 (GPC3) is a cell surface heparan sulfate proteoglycan that is being evaluated as an emerging therapeutic target in hepatocellular carcinoma (HCC). GPC3 has been shown to interact with several extracellular signaling molecules, including Wnt, HGF, and Hedgehog. Here, we reported a cell surface transmembrane protein (FAT1) as a new GPC3 interacting protein. The GPC3 binding region on FAT1 was initially mapped to the C-terminal region (Q14517, residues 3662-4181), which covered a putative receptor tyrosine phosphatase (RTP)-like domain, a Laminin G-like domain, and five EGF-like domains. Fine mapping by ELISA and flow cytometry showed that the last four EGF-like domains (residues 4013-4181) contained a specific GPC3 binding site, whereas the RTP domain (residues 3662-3788) and the downstream Laminin G-2nd EGF-like region (residues 3829-4050) had non-specific GPC3 binding. In support of their interaction, GPC3 and FAT1 behaved concomitantly or at a similar pattern, e.g. having elevated expression in HCC cells, being up-regulated under hypoxia conditions, and being able to regulate the expression of EMT-related genes Snail, Vimentin, and E-Cadherin and promoting HCC cell migration. Taken together, our study provides the initial evidence for the novel mechanism of GPC3 and FAT1 in promoting HCC cell migration.
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Registered trials
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