ArticleThe Journal of biological chemistry2026
The ASC-c isoform as a modulator of inflammasome activation: Insights into molecular mechanisms and therapeutic applications.
Article in The Journal of biological chemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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Who cites it
1 citing paper in PubMed.
- Inflammasome-associated pyroptosis and tumor angiogenesis in prostate cancer.Iranian journal of basic medical sciences · 2026Review
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Authors and funding
7 authors.
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Abstract
Canonical inflammasome assembly is driven by interactions between sensors and effector procaspase-1, primarily mediated by the adaptor ASC. Homotypic interactions between Death Domains pyrin (PYD) and caspase recruitment and activation domain (CARD) lead to sensor and ASC oligomerization, along with the recruitment of procaspase-1. ASC self-association is essential for inflammasome activation, which initiates inflammatory responses. Therefore, uncontrolled inflammasome activation contributes to chronic inflammatory diseases. ASC-c, an isoform of ASC, acts as a negative regulator of the inflammasome. To better understand ASC-c's regulatory role, we examined its structural properties and interactions with ASC. Our nuclear magnetic resonance data show that ASC-c's CARD is properly folded, whereas the PYD consists of two α-helices instead of the six-helix bundle typical of Death Domains. In addition, a chemical shift perturbation analysis indicates that ASC-c interacts with ASC. We obtained transmission electron micrographs revealing that ASC-c polymerizes into filaments and filament bundles, which display greater heterogeneity than those of ASC based on dynamic light scattering. Overall, our results suggest that ASC-c binding to ASC can have an impact on ASC self-association, thereby affecting inflammasome assembly. Based on these findings, we designed a peptide encompassing the two helices of the ASC-c PYD to target ASC for therapeutic purposes. We demonstrate the interaction between the peptide and ASC by fluorescence anisotropy and show the stability of the complex by molecular dynamics simulations. Finally, cell-based assays measuring inflammasome activation indicate an inhibitory effect of the ASC-c peptide, pointing to its potential use in drug design.
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