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cGAS inhibition delays TDP-43-driven ALS Pathogenesis

Liu, Y.; Feng, W.; Aikedan, A. A.; Lee, S.-I.; Bhagwat, M.; Nagiri, R. K.; Wong, M. Y.; Amin, S.; Qu, W.; Zhu, J.; Wang, S.-Y.; Ye, P.; Norman, K.; Coronas-Samano, G. B.; Olah, M.; Tilgner, H. U.; Sinha, S.; Gan, L.

2026-02-26 neuroscience
10.64898/2026.02.24.707791 bioRxiv
Show abstract

Amyotrophic lateral sclerosis (ALS) is a fatal neurodegenerative disorder marked by motor neuron loss and cytoplasmic mislocalization of TAR DNA-binding protein 43 (TDP-43), a key regulator of RNA splicing. However, the upstream modulators of this process remain poorly defined. Here we identify cyclic GMP-AMP synthase (cGAS) as a central mediator of TDP-43 pathology and associated mis-splicing. cGAS expression was elevated in ALS patient brains and enriched across activated microglia. In human iPSC-derived microglia-motor neuron co-cultures, neuronal TDP-43 pathology triggered microglial cGAS activation, whereas pharmacological inhibition with a potent human cGAS inhibitor reduced phosphorylated TDP-43, restored lysosomal and phagocytic programs, normalized microglial reactivity, and reversed TDP-43-associated RNA splicing defects. In vivo, cGAS inhibition in TDP-43 Q331K mice reversed widespread RNA splicing abnormalities across neurons and oligodendrocyte lineage cells, attenuated neurodegenerative pathology, and preserved motor function. Together, these findings identify cGAS as a druggable upstream regulator linking innate immune signaling to TDP-43-dependent RNA mis-splicing and neurodegeneration, and establish cGAS inhibition as a promising therapeutic strategy for ALS.

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