ArticleThe Journal of biological chemistry2020
Cryo-electron microscopy structure and potential enzymatic function of human six-transmembrane epithelial antigen of the prostate 1 (STEAP1).
Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 53 citations in OpenAlex.
- STEAP1-targeted strategies in advanced prostate cancer: a review on therapeutic and diagnostic implications.Prostate cancer and prostatic diseases · 2026Review
- STEAP1 Suppresses Oral Squamous Cell Carcinoma by Targeting Wnt/β-Catenin Signalling and EMT.Cancer medicine · 2026Article
- Development of a STEAP1-Targeted Prostate Cancer Specific Antibody Drug Conjugate Platform with Immunostimulatory Properties.Research square · 2026Article
- A cost-effective 200 kV cryo-EM core facility for high resolution single particle analysis.Methods in microscopy · 2026Article
- Progress in targeted therapy for prostate cancer via cell surface proteins (Review).Biomedical reports · 2026Review
- Armoring STEAP1 CAR T cells with IL-18 potentiates antitumor activity in Ewing sarcoma.bioRxiv : the preprint server for biology · 2025Article
- CAR-T Cell Therapy for Prostate Cancer: Current Advances and Future Perspectives.Biomedicines · 2025Review
- Studies of the membrane-bound flavocytochrome MsrQ flavin mononucleotide (FMN)-binding site reveal an unexpected ubiquinone cofactor.The FEBS journal · 2025Article
- The Role of STEAP1 in Prostate Cancer: Implications for Diagnosis and Therapeutic Strategies.Biomedicines · 2025Review
- Prion protein promotes copper toxicity in Wilson disease.Nature communications · 2025Article
- The application of emerging immunotherapy in the treatment of prostate cancer: progress, dilemma and promise.Frontiers in immunology · 2025Review
- STEAP2 promotes hepatocellular carcinoma progression via increased copper levels and stress-activated MAP kinase activity.Scientific reports · 2024Article
- Tumor Heterogeneity of STEAP4 in Malignant Progression of Oral Squamous Cell Carcinoma.Journal of Cancer · 2024Article
- Cryo-electron microscopy-based drug design.Frontiers in molecular biosciences · 2024Review
- Article
- Inhibition of STEAP1 ameliorates inflammation and ferroptosis of acute lung injury caused by sepsis in LPS-induced human pulmonary microvascular endothelial cells.Molecular biology reports · 2023Article
- Targeting advanced prostate cancer with STEAP1 chimeric antigen receptor T cell and tumor-localized IL-12 immunotherapy.Nature communications · 2023Article
- Specific Six-Transmembrane Epithelial Antigen of the Prostate 1 Capture with Gellan Gum Microspheres: Design, Optimization and Integration.International journal of molecular sciences · 2023Article
- Targeting STEAP1 as an anticancer strategy.Frontiers in oncology · 2023Review
- STEAP2 promotes osteosarcoma progression by inducing epithelial-mesenchymal transition via the PI3K/AKT/mTOR signaling pathway and is regulated by EFEMP2.Cancer biology & therapy · 2022Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Six-transmembrane epithelial antigen of the prostate 1 (STEAP1) is an integral membrane protein that is highly up-regulated on the cell surface of several human cancers, making it a promising therapeutic target to manage these diseases. It shares sequence homology with three enzymes (STEAP2-STEAP4) that catalyze the NADPH-dependent reduction of iron(III). However, STEAP1 lacks an intracellular NADPH-binding domain and does not exhibit cellular ferric reductase activity. Thus, both the molecular function of STEAP1 and its role in cancer progression remain elusive. Here, we present a ∼3.0-Å cryo-EM structure of trimeric human STEAP1 bound to three antigen-binding fragments (Fabs) of the clinically used antibody mAb120.545. The structure revealed that STEAP1 adopts a reductase-like conformation and interacts with the Fabs through its extracellular helices. Enzymatic assays in human cells revealed that STEAP1 promotes iron(III) reduction when fused to the intracellular NADPH-binding domain of its family member STEAP4, suggesting that STEAP1 functions as a ferric reductase in STEAP heterotrimers. Our work provides a foundation for deciphering the molecular mechanisms of STEAP1 and may be useful in the design of new therapeutic strategies to target STEAP1 in 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.