ReviewFrontiers in immunology2025
Chromatin-associated cullin-RING E3 ubiquitin ligases: keeping transcriptionally active NF-κB in check.
Review in Frontiers in immunology, 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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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Authors and funding
6 authors.
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Abstract
Nuclear factor-κB (NF-κB) constitutes a family of transcription factors that serve as a critical regulatory hub, dynamically orchestrating inflammatory and immune responses to maintain homeostasis and protect against pathogenic threats. Persistent activation of NF-κB has been implicated in the pathogenesis of various inflammatory diseases and cancer. A critical mechanism to prevent excessive inflammation and its harmful effects is the timely termination of NF-κB's transcriptional activity on target genes. This termination can be facilitated through the ubiquitination and subsequent proteasomal degradation of chromatin-bound RelA, the most active subunit of NF-κB. Several multi-subunit cullin-RING E3 ubiquitin ligases, composed of elongin B/C, cullin2/5, and SOCS-box proteins, have been identified to target RelA for degradation. These E3s, known as ECS complexes, use SOCS-box proteins as substrate-recognizing subunits to engage RelA. SOCS1 is the first identified SOCS-box member that functions in ECS
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