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Dual mechanism of human ATG10S in suppressing MEF2A-driven pro-inflammatory responses. First, ATG10S directly binds to MEF2A and promotes its targeting to autolysosomes for degradation. Second, in the nucleus, ATG10S competes with MAPK7 for binding to MEF2A, thereby disrupting the TLR4-MAPK7-MEF2A signaling axis and suppressing MEF2A transcriptional activity. Together, these dual mechanisms effectively suppress the overexpression of pro-inflammatory cytokines (IFNA, IFNG, IL1B, IL6, TNF, IL8, and CCL2) induced by SARS-CoV-2 S protein or LPS. This diagram was generated using BioRender.com.

Journal: Autophagy

Article Title: Dual mechanism of human ATG10S in suppressing MEF2A-Driven pro-inflammatory responses

doi: 10.1080/15548627.2026.2676074

Figure Lengend Snippet: Dual mechanism of human ATG10S in suppressing MEF2A-driven pro-inflammatory responses. First, ATG10S directly binds to MEF2A and promotes its targeting to autolysosomes for degradation. Second, in the nucleus, ATG10S competes with MAPK7 for binding to MEF2A, thereby disrupting the TLR4-MAPK7-MEF2A signaling axis and suppressing MEF2A transcriptional activity. Together, these dual mechanisms effectively suppress the overexpression of pro-inflammatory cytokines (IFNA, IFNG, IL1B, IL6, TNF, IL8, and CCL2) induced by SARS-CoV-2 S protein or LPS. This diagram was generated using BioRender.com.

Article Snippet: Recombinant wild-type SARS-CoV-2 S protein (isolate: 2019-nCoV, 40,591-V08B1) was obtained from Sino Biological (Beijing, China).

Techniques: Binding Assay, Activity Assay, Over Expression, Generated