Structural mechanism of Necrocide 1 activation of human TRPM4 that triggers necrosis by sodium overload

The small molecule Necrocide 1 (NC1) constitutively activates human TRPM4, triggering Na⁺ influx and leading to necrotic cell death, a process termed Necrosis by Sodium Overload (NECSO). NC1 activation is specific to human TRPM4 and does not affect most of the other mammalian TRPM4 orthologs. Here, we elucidate the molecular mechanism underlying NC1 activation and its species-specific selectivity for human TRPM4 using a combination of single-particle cryo-EM, electrophysiology, and cell death assays. We identify the NC1-binding site and the key molecular determinants responsible for channel activation. In addition, we explain the insensitivity of mouse TRPM4 to NC1 and pinpoint specific residues that define NC1 specificity for human TRPM4. Given the upregulation of TRPM4 in various human cancers, our mechanistic insights into NC1 activation and specificity provide a framework for the potential development of cancer therapeutics targeting TRPM4-mediated necrosis.

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Publication Details

Journal
Nature Communications
Published
2026-06-24
DOI
https://doi.org/10.1038/s41467-026-74814-2
Primary Topic
Ion Channels and Receptors
Type
article
Field-Weighted Citation Impact
0.00

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article

Structural mechanism of Necrocide 1 activation of human TRPM4 that triggers necrosis by sodium overload

Jianghuang Wang, Qing Zhong, Weizhong Zeng, Celso M. Teixeira‐Duarte et al.
Nature Communications
Ion Channels and Receptors
article

Structural mechanism of Necrocide 1 activation of human TRPM4 that triggers necrosis by sodium overload

Jianghuang Wang, Qing Zhong, Weizhong Zeng, Celso M. Teixeira‐Duarte, Youxing Jiang, Wan Fu, Ziye Zhao, Xinzhe Jiang
article en

Abstract

The small molecule Necrocide 1 (NC1) constitutively activates human TRPM4, triggering Na⁺ influx and leading to necrotic cell death, a process termed Necrosis by Sodium Overload (NECSO). NC1 activation is specific to human TRPM4 and does not affect most of the other mammalian TRPM4 orthologs. Here, we elucidate the molecular mechanism underlying NC1 activation and its species-specific selectivity for human TRPM4 using a combination of single-particle cryo-EM, electrophysiology, and cell death assays. We identify the NC1-binding site and the key molecular determinants responsible for channel activation. In addition, we explain the insensitivity of mouse TRPM4 to NC1 and pinpoint specific residues that define NC1 specificity for human TRPM4. Given the upregulation of TRPM4 in various human cancers, our mechanistic insights into NC1 activation and specificity provide a framework for the potential development of cancer therapeutics targeting TRPM4-mediated necrosis.

Nature Communications
Howard Hughes Medical Institute (US), Southwestern Medical Center (US), Shanghai Ninth People's Hospital (CN), Ministry of Education (TH), The University of Texas Southwestern Medical Center (US)
Howard Hughes Medical Institute, Cancer Prevention and Research Institute of Texas, University of Texas Southwestern Medical Center, National Natural Science Foundation of China, Ministry of Science and Technology of the People's Republic of China, National Natural Science Foundation of China-Yunnan Joint Fund
Good health and well-being
Openalex Percentile: Top 8%
Ion Channels and Receptors
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