ArticleNeoplasia (New York, N.Y.)2020
AGO2 phosphorylation by c-Src kinase promotes tumorigenesis.
Article in Neoplasia (New York, N.Y.), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 16 citations in OpenAlex.
- Targeting the TRIM25-AGO2-miR-148b-5p-ABCC1 axis overcomes chemoresistance in non-small cell lung cancer.Cell death & disease · 2026Article
- Partners in Silencing: Decoding the Mammalian Argonaute Interactome.Non-coding RNA · 2025Review
- Recent Advances in the miRNA-Mediated Regulation of Neuronal Differentiation and Death.Neuromolecular medicine · 2024Review
- Loss of Lamin A leads to the nuclear translocation of AGO2 and compromised RNA interference.Nucleic acids research · 2024Article
- Phosphorylation of AGO2 by TBK1 Promotes the Formation of Oncogenic miRISC in NSCLC.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Regulation of microRNA expression by the adaptor protein GRB2.Scientific reports · 2023Article
- KRAS Hijacks the miRNA Regulatory Pathway in Cancer.Cancer research · 2023Article
- Argonaute 2 modulates EGFR-RAS signaling to promote mutantPNAS nexus · 2022Article
- Hypoxia regulates overall mRNA homeostasis by inducing MetNature communications · 2021Article
- Frontiers of MicroRNA Signature in Non-small Cell Lung Cancer.Frontiers in cell and developmental biology · 2021Review
- From the Argonauts Mythological Sailors to the Argonautes RNA-Silencing Navigators: Their Emerging Roles in Human-Cell Pathologies.International journal of molecular sciences · 2020Review
Corrections and comments
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Authors and funding
10 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Numerous studies have reported that c-Src is highly expressed with high tyrosine kinase activity in a variety of tumors. However, it remains unclear whether c-Src contributes to the miRNA pathway. Here, we report that c-Src can interact with and phosphorylate AGO2, a core component of RISC complex, at tyr 393, tyr 529 and tyr749. Mechanistically, it is confirmed that c-Src phosphorylation of AGO2 at tyr393 reduces its binding to DICER, thereby suppressing the maturation of long-loop pre-miR-192. However, the other two phosphorylation sites don't work on this function. Significantly, Ectopic expression of wild-type AGO2, but not the three tyrosine site mutants, has an obvious tumor-promoting effect in vitro and in vivo, which function could be blocked thoroughly by treatment with c-Src kinase inhibitor, Saracatinib. Our findings identify AGO2 as c-Src target and c-Src phosphorylation of AGO2 may therefore play a potential role during tumor progress.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.