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TitleITGB1 Regulates Triple-Negative Breast Cancer Development by Modulating the Tumor Microenvironment.
Journal, issue, pagesAdv Sci (Weinh), Page e13672, Year 2026
Publish dateFeb 3, 2026
AuthorsNuozi Song / Siqi Chen / Lei Wang / Jessica Dang / Xu Cao / Stephanie Singh / Lu Yang / Jinhui Wang / Steven T Rosen / Yingyu Wang / Chun-Wei D Chen / Cheng Zhang / Mingye Feng /
PubMed AbstractTumorigenesis and metastasis are frequently attributed to the intricate interplay between cancer cells and the tumor microenvironment (TME). Comprehending the mechanisms and key regulators of cancer- ...Tumorigenesis and metastasis are frequently attributed to the intricate interplay between cancer cells and the tumor microenvironment (TME). Comprehending the mechanisms and key regulators of cancer-immune crosstalk in the TME is imperative for developing efficacious immunotherapy. Through a series of in vivo CRISPR screens, we identified tumor-intrinsic ITGB1 as a critical regulator of triple-negative breast cancer (TNBC) development and deciphered its underlying mechanisms. Tumoral ITGB1 facilitated the establishment of pro-tumorigenic TME by orchestrating tumor-associated myeloid populations. Suppressing ITGB1 favored the enrichment of anti-tumorigenic myeloid cells and enhanced infiltration of CD4 and CD8 T cells, culminating in superior antitumor effects. CRISPR scanning pinpointed a previously unrecognized functional domain essential for ITGB1's pro-tumorigenic activity. This domain is distinct from all known ligand-binding sites in ITGB1. An antibody capable of sterically blocking this domain significantly impaired TNBC progression. These findings position tumoral ITGB1 as a promising therapeutic target for reprogramming the TME from a pro- to an anti-tumorigenic state, thereby effectively inhibiting TNBC development. Our study uncovers a novel mechanism of TNBC development and provides a unique therapeutic strategy for targeting ITGB1 in TNBC treatment.
External linksAdv Sci (Weinh) / PubMed:41632816
MethodsEM (single particle)
Resolution2.54 Å
Structure data

49184

9nab

EMDB-49184, PDB-9nab:
Cryo-EM structure of the alpha5beta1 integrin headpiece with OS2966 Fab
Method: EM (single particle) / Resolution: 2.54 Å

Source
  • HEk293 (human)
  • homo sapiens (human)
  • mus musculus (house mouse)
KeywordsIMMUNE SYSTEM / Integrin antibody

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