Two back-to-back papers published in Nature on Sept. 10, 2025, shed new light on the unexpected role of neurons in shaping the evolution of small-cell lung cancer (SCLC). It’s already known that, in gliomas, cerebral cancer cells actively damage axons, contributing to tumor progression through direct neural disruption. Comparable nerve-tumor interactions have been reported in peripheral cancers, where tumor-induced nerve disruption promotes inflammation and an immunosuppressive microenvironment linked to immunotherapy resistance.

N6-methyladenosine (m6A) modification, mainly controlled by the m6A methyltransferase METTL3, is crucial for RNA regulation and the development of leukemia. However, how METTL3 stability and function are regulated after translation is not fully understood. Since O-GlcNAcylation commonly modifies nuclear and cytosolic proteins, researchers have hypothesized that METTL3 may be O-GlcNAcylated, affecting its stability and oncogenic activity in myeloid malignancies.

Glioblastoma multiforme (GBM) is the most aggressive and common type of brain cancer in adults, with a dismal prognosis despite current treatments. Previous work found that neurodevelopmental pathways drive glioma tumor initiation, maintenance and progression through fetal oncogenes, which are active in development and cancer but largely absent in adult tissues, offering precise therapeutic targets with minimal off-target effects.

Osteosarcoma, the most common bone cancer in children and young adults, has poor outcomes after relapse with only ~18% 5-year survival, underscoring the urgent need for new therapies. Researchers from New York Medical College and colleagues have now demonstrated a new strategy to improve the efficacy of natural killer (NK) cell-based immunotherapy for osteosarcoma.

Immuto Scientific Inc. has closed an $8 million seed 2 financing round and entered into a drug discovery collaboration with Daiichi Sankyo Co. Ltd. Immuto applies its target discovery platform and structural epitope‑mapping engine to identify disease‑specific surface protein conformations.