Direct activation of SARM1 by dsDNA is not supported by biochemical and cellular evidence

Sterile alpha and Toll/interleukin-1 receptor motif–containing protein 1 (SARM1) is a NAD + -consuming enzyme that drives axon degeneration and is activated by changes in the NMN/NAD + ratio. A recent study proposed that cytosolic double-stranded DNA (dsDNA) directly binds SARM1’s TIR domain, activating it independently of this canonical mechanism. Here, we evaluate dsDNA-dependent SARM1 activation using purified SARM1, biochemical and biophysical assays, primary neurons, and cellular pharmacology. Across multiple platforms, dsDNA does not stimulate SARM1 NADase activity, promote higher-order assembly, or generate the metabolic signature of activated SARM1. When effects are observed, they are weak, context-dependent, and inconsistent across assays, and do not support a defined activation mechanism. In cells, dsDNA induces NAD + depletion through PARP-dependent pathways independently of SARM1. The reported DNA-binding mutant (3KE-SARM1) is nonfunctional in canonical SARM1 activation paradigms such as axotomy and therefore cannot be used to infer dsDNA activation mechanisms. Together, these findings do not support a model in which SARM1 is directly activated by dsDNA.

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Publication Details

Journal
Proceedings of the National Academy of Sciences
Published
2026-09-11
DOI
https://doi.org/10.1073/pnas.2620112123
Primary Topic
Sirtuins and Resveratrol in Medicine
Type
article
Field-Weighted Citation Impact
0.00

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article

Direct activation of SARM1 by dsDNA is not supported by biochemical and cellular evidence

Jeffrey Milbrandt, Mitchell Sorbello, Giuseppe Orsomando, Aaron DiAntonio et al.
Proceedings of the National Academy of Sciences
Sirtuins and Resveratrol in Medicine
article

Direct activation of SARM1 by dsDNA is not supported by biochemical and cellular evidence

Jeffrey Milbrandt, Mitchell Sorbello, Giuseppe Orsomando, Aaron DiAntonio, Weixi Gu, Biswa Prasanna Mishra, Boštjan Kobe, Yong Zhao, Yuefeng Jiang, Thomas Ve, Allison Kao, Qinyi Zhou, Veronika Masic, Robi D. Mitra, Xiaodong Wang, Zhe Zhang, Wenbin Zhang, Jian Yuan Yang, Paige Harten, A. Joseph Bloom
article en

Abstract

Sterile alpha and Toll/interleukin-1 receptor motif–containing protein 1 (SARM1) is a NAD + -consuming enzyme that drives axon degeneration and is activated by changes in the NMN/NAD + ratio. A recent study proposed that cytosolic double-stranded DNA (dsDNA) directly binds SARM1’s TIR domain, activating it independently of this canonical mechanism. Here, we evaluate dsDNA-dependent SARM1 activation using purified SARM1, biochemical and biophysical assays, primary neurons, and cellular pharmacology. Across multiple platforms, dsDNA does not stimulate SARM1 NADase activity, promote higher-order assembly, or generate the metabolic signature of activated SARM1. When effects are observed, they are weak, context-dependent, and inconsistent across assays, and do not support a defined activation mechanism. In cells, dsDNA induces NAD + depletion through PARP-dependent pathways independently of SARM1. The reported DNA-binding mutant (3KE-SARM1) is nonfunctional in canonical SARM1 activation paradigms such as axotomy and therefore cannot be used to infer dsDNA activation mechanisms. Together, these findings do not support a model in which SARM1 is directly activated by dsDNA.

Proceedings of the National Academy of SciencesVol. 123(37)
Griffith University (AU), Marche Polytechnic University (IT), The University of Queensland (AU), Chinese University of Hong Kong (HK), National Institute of Biological Sciences, Beijing (CN), Institute for Biomedicine (IT), AgriBio (AU), Center for Life Sciences (CN)
National Natural Science Foundation of China, Ministry of Science and Technology of the People's Republic of China, National Institutes of Health, National Health and Medical Research Council, Beijing Municipal Natural Science Foundation
Openalex Percentile: Top 14%
Sirtuins and Resveratrol in Medicine
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