High-throughput spheroid profiling reveals BMP-driven rewiring of glioma cell death responses.

Weaverly Colleen Lee, Jennifer J Salinas, Aastha Gautam, Dimitri Cadet, Matei A Banu, David A Nathanson, Scott J Dixon

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In one paragraph

Article in bioRxiv : the preprint server for biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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7 authors.

Weaverly Colleen LeeDepartment of Biology, Stanford University, Stanford, CA 94305, USA.

Jennifer J SalinasDepartment of Molecular & Medical Pharmacology, University of California at Los Angeles, Los Angeles, CA 90095, USA.

Aastha GautamDepartment of Biology, Stanford University, Stanford, CA 94305, USA.

Dimitri CadetDepartment of Molecular & Medical Pharmacology, University of California at Los Angeles, Los Angeles, CA 90095, USA.

Matei A BanuDepartment of Neurosurgery, Stanford University School of Medicine, Stanford, CA 94305, USA.

David A NathansonDepartment of Molecular & Medical Pharmacology, University of California at Los Angeles, Los Angeles, CA 90095, USA.

Scott J DixonDepartment of Biology, Stanford University, Stanford, CA 94305, USA.ORCID 0000-0001-6230-8199

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The mechanisms regulating glioma cell death are poorly understood. Here, we developed a high-throughput method to study cell death in patient-derived glioblastoma (GBM) and diffuse intrinsic pontine glioma (DIPG) spheroids. Using this method, we systematically profiled how extracellular ligands modulate compound-induced cell death. We find that bone morphogenetic protein 2 (BMP2) and BMP4 potently rewire cell death sensitivity. These ligands suppress killing by standard-of-care DNA alkylating agents and kinase inhibitors by inhibiting cell cycle progression. Simultaneously, BMP2/4 prime spheroids for lipid-dependent necrosis (LiDN), a palmitate-dependent form of non-apoptotic cell death that can be triggered by the clinical drug candidate tegavivint. Activating mutations in the BMP receptor ACVR1, found in ~25% of DIPG tumors, are sufficient to prime cells for LiDN in the absence of BMP ligand. Together, these findings identify a cell death switch that can be activated in glioma cells by BMP signaling.

Indexed as

BMP2BMP4cell deathcell statelipidnecrosispalmitatepalmitoylation

Identifiers

PMID42818713

DOI10.64898/2026.09.10.750657

PMCPMC13622622

What Socratic holds

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Read underepoch 390

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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 Socratic graph.