Targeting the α4–α5 dimerization interface of K-RAS inhibits tumor formation in vivo
Open accessAbstract
RAS genes are the most commonly mutated oncogenes in human cancers. Despite tremendous efforts over the past several decades, however, RAS-specific inhibitors remain elusive. Thus, targeting RAS remains a highly sought-after goal of cancer research. Previously, we have reported a new approach to inhibit RAS-dependent signaling and transformation in vitro by targeting the α4-α5 dimerization interface with a novel RAS-specific monobody termed NS1. Expression of NS1 inhibits oncogenic K-RAS and H-RAS signaling and transformation in vitro. Here, we evaluated the efficacy of targeting RAS dimerization as an approach to inhibit tumor formation in vivo. Using a doxycycline (DOX)-regulated NS1 expression system, we demonstrate that DOX-induced NS1 inhibited oncogenic K-RAS-driven tumor growth in vivo. Furthermore, we observed context-specific effects of NS1 on RAS-mediated signaling in 2D vs 3D growth conditions. Finally, our results highlight the potential therapeutic efficacy of targeting the α4-α5 dimerization interface as an approach to inhibit RAS-driven tumors in vivo.
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NS1 disrupts the self-binding of HRAS and KRAS by directly binding to the α4-α5 interface, reducing activation of downstream pathways and inhibiting cell proliferation.
“Without interfering with RAS localization and GTPase activity, NS1 disrupts the self-binding of HRAS and KRAS by directly binding to the α4–α5 interface, reducing the activation of downstream pathways and inhibiting cell proliferation [30, 63, 64].”
From Targeting KRAS mutant cancers: from druggable therapy to drug resistance (2022) · cites this paper as [64]
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SAIMSARA (2026) · SAIMSARA Journal · doi:10.62487/saimsaradc4d1e0f
- Authors
- Khan, I., Spencer-Smith, R., & O’Bryan, J. P.
- Affiliations
- Medical University of South Carolina (US)
- University of Illinois Chicago (US)
- Corresponding author
- O’Bryan, John P.
- Venue
- Oncogene
- Published
- 2018-12-20
- Volume
- 38
- Issue
- 16
- Pages
- 2984-2993
- ISSN
- 0950-9232 (ISSN-L)
- 1476-5594
- PMC
- PMC6474814
- OpenAlex
- W2904125429
- Cited by
- 54
- References
- 27
- Citations by year
- 2026: 2 · 2025: 2 · 2024: 5 · 2023: 7 · 2022: 14 · 2021: 11 · 2020: 9 · 2019: 4
- FWCI
- 2.13
- Type
- journal article
- Language
- en
- Update notices
- correction (2019-02-01)
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Oncogene (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- U.S. Department of Health & Human Services | National Institutes of Health (CA192822)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Melanoma and MAPK Pathways
- Keywords
- KRAS, NS1 protein, RAS inhibitors, oncogenic Ras signaling, tumor growth inhibition, H-Ras, cancer therapy
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