ArticleNature chemical biology2020
Targeting the interaction of AIMP2-DX2 with HSP70 suppresses cancer development.
Article in Nature chemical biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 46 citations in OpenAlex.
- TSG101 Promotes SIAH1 Auto-Ubiquitination to Drive Migration and Invasion in Hepatocellular Carcinoma Cells.Journal of cellular and molecular medicine · 2026Article
- The Dual Role of Survival Genes in Neurons and Cancer Cells: a Strategic Clinical Application of DX2 in Neurodegenerative Diseases and Cancer.Biomolecules & therapeutics · 2025Review
- The Confluence of Nanotechnology and Heat Shock Protein 70 in Pioneering Glioblastoma Multiforme Therapy: Forging Pathways Towards Precision Targeting and Transformation.Advances in pharmacological and pharmaceutical sciences · 2025Review
- Protein isoform-centric therapeutics: expanding targets and increasing specificity.Nature reviews. Drug discovery · 2024Review
- Deficiency of SIAH1 promotes the formation of filopodia by increasing the accumulation of FASN in liver cancer.Cell death & disease · 2024Article
- Identification and structure of AIMP2-DX2 for therapeutic perspectives.BMB reports · 2024Review
- Synthesis and discovery of the first potent proteolysis targeting chimaera (PROTAC) degrader of AIMP2-DX2 as a lung cancer drug.Journal of enzyme inhibition and medicinal chemistry · 2023Article
- The function of alternative splicing in the proteome: rewiring protein interactomes to put old functions into new contexts.Nature structural & molecular biology · 2023Review
- Cathepsin K promotes the proliferation of hepatocellular carcinoma cells through induction of SIAH1 ubiquitination and degradation.iScience · 2023Article
- Sandwich-like electrochemical aptasensing of heat shock protein 70 kDa (HSP70): Application in diagnosis/prognosis of coronavirus disease 2019 (COVID-19).Analytica chimica acta · 2023Article
- Advances in Brain Tumor Therapy Based on the Magnetic Nanoparticles.International journal of nanomedicine · 2023Review
- Article
- AIMP2-DX2 provides therapeutic interface to control KRAS-driven tumorigenesis.Nature communications · 2022Article
- Functional and pathologic association of aminoacyl-tRNA synthetases with cancer.Experimental & molecular medicine · 2022Review
- SIAH1 reverses chemoresistance in epithelial ovarian cancer via ubiquitination of YBX-1.Oncogenesis · 2022Article
- Roburic Acid Targets TNF to Inhibit the NF-κB Signaling Pathway and Suppress Human Colorectal Cancer Cell Growth.Frontiers in immunology · 2022Article
- The Clinical Prediction Value of the Ubiquitination Model Reflecting the Immune Traits in LUAD.Frontiers in immunology · 2022Article
- HSP70 and HSP90 in Cancer: Cytosolic, Endoplasmic Reticulum and Mitochondrial Chaperones of Tumorigenesis.Frontiers in oncology · 2022Review
- Long noncoding RNAMolecular therapy. Nucleic acids · 2021Article
- tRNA Metabolism and Lung Cancer: Beyond Translation.Frontiers in molecular biosciences · 2021Review
Corrections and comments
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Authors and funding
17 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A tumorigenic factor, AIMP2 lacking exon 2 (AIMP2-DX2), is often upregulated in many cancers. However, how its cellular level is determined is not understood. Here, we report heat-shock protein HSP70 as a critical determinant for the level of AIMP2-DX2. Interaction of the two factors was identified by interactome analysis and structurally determined by X-ray crystallography and NMR analyses. HSP70 recognizes the amino (N)-terminal flexible region, as well as the glutathione S-transferase domain of AIMP2-DX2, via its substrate-binding domain, thus blocking the Siah1-dependent ubiquitination of AIMP2-DX2. AIMP2-DX2-induced cell transformation and cancer progression in vivo was further augmented by HSP70. A positive correlation between HSP70 and AIMP2-DX2 levels was shown in various lung cancer cell lines and patient tissues. Chemical intervention in the AIMP2-DX2-HSP70 interaction suppressed cancer cell growth in vitro and in vivo. Thus, this work demonstrates the importance of the interaction between AIMP2-DX2 and HSP70 on tumor progression and its therapeutic potential against cancer.
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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.