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Updated: Nov 20, 2025

Identifying the Binding Proteins of Small Ligands with the Differential Radial Capillary Action of Ligand Assay DRaCALA
Published on: March 19, 2021
Identification of Radil as a Ras binding partner and putative activator
Byeong Hyeok Choi1, Ziyue Kou1, Tania Marlyn Colon1
1Department of Environmental Medicine, New York University Langone Medical Center, New York, New York, USA.
Researchers identified Radil as a novel regulator of Ras signaling. This protein interacts with Ras, influencing cell adhesion, migration, and proliferation, offering new targets for anticancer drug development.
Area of Science:
- Oncology
- Molecular Biology
- Cell Biology
Background:
- Ras genes are frequently mutated oncogenes in human cancers.
- Current therapies targeting Ras proteins are limited.
- Identifying novel regulators of Ras signaling is crucial for developing new anticancer drugs.
Purpose of the Study:
- To identify novel proteins associated with KRas.
- To characterize the role of Radil in Ras signaling pathways.
- To explore Radil as a potential therapeutic target for Ras-related cancers.
Main Methods:
- Affinity-pulldown assays combined with mass spectrometry to identify KRas-interacting proteins.
- Western blotting and co-immunoprecipitation to confirm protein interactions.
- Cell-based assays to assess the impact of Radil modulation on cell signaling, proliferation, invasion, and migration.
Main Results:
- Radil was identified as a novel KRas-interacting protein, binding to all Ras isoforms with a preference for KRas.
- Radil interacts with GTP-bound Ras, suggesting a role in Ras activation.
- Radil knockdown impaired Ras downstream signaling, reduced cell proliferation and invasion, and inhibited cell adhesion and migration.
Conclusions:
- Radil is a significant regulator of Ras signaling, impacting cell adhesion, migration, and epithelial-mesenchymal transition.
- Radil represents a promising new target for the development of anticancer drugs against Ras-driven malignancies.
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