ArticleNeurochemical research2025
Effects of E2F1 Point Acetylation at Lysine 117 or 125 on Neuronal Apoptosis After Ischemic Injury.
Article in Neurochemical research, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Transcription factors of the E2F1 family belong to those identified to be in the center of signaling cascade responsible for the propagation of apoptosis, including stroke-induced ischemia conditions in the brain. E2F1 activity is mediated by its binding to DP1 and retinoblastoma proteins and its phosphorylation and acetylation. We have studied the effects of E2F1 point acetylation at lysins 117 and 125 on its interaction with retinoblastoma and its role in penumbra cell fate after photothrombotic stroke. E2F1, in complex with retinoblastoma, is mainly unacetylated or acetylated at lysine 125 by PCAF. The formation of this complex is associated with the upregulation of E2F1 after stroke due to pRb protecting E2F1 from degradation vie ubiquitin-proteasome mechanism. Point acetylation of E2F1 at lysine 117 contributes to increased neuronal apoptosis induces by oxidative stress and is associated with inhibition of the "S"-site binding of retinoblastoma. Acetylation levels of E2F1 at K125 is regulated by HDAC1. The identification of selective deacetylase for E2F1 at lysine 117 would provide new means for the modulation of oxidative stress-induced neuronal apoptosis.
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