ArticleScientific reports2017
MKRN2 is a novel ubiquitin E3 ligase for the p65 subunit of NF-κB and negatively regulates inflammatory responses.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers, 1 of them a synthesis that pooled it.
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Who cites it
44 citing papers in PubMed, 1 synthesis or guideline pooled it, 73 citations in OpenAlex.
- Multi-ancestry and multi-trait genome-wide association meta-analyses inform clinical risk prediction for systemic lupus erythematosus.Nature communications · 2023Pooled it
- The E3 ligase MKRN2 prevents DRiP accumulation in stress granules and maintains granulostasis.EMBO reports · 2026Article
- PDLIM2 acts as a central regulator of ubiquitination, immune signaling, and mitochondrial metabolism in lung cancer suppression (Review).International journal of oncology · 2026Review
- Integrating whole-genome resequencing data reveals adaptive selection signatures under extreme environments of goat populations in China.BMC genomics · 2026Article
- MKRN2 enhances hepatocellular carcinoma proliferation through the p38 MAPK pathway.Human cell · 2026Article
- Article
- Liquid-liquid phase separation couples MKRN2-mediated ubiquitination of CSDE1 with neurodevelopmental disorders.Frontiers in cellular neuroscience · 2026Article
- The RNA-binding E3 ligase MKRN2 selectively disrupts Il6 translation to restrain inflammation.Nature immunology · 2025Article
- Transcriptional Landscape and Biomarker Discovery for Endoplasmic Reticulum Stress in Alzheimer's Disease: An Ex Vivo Study Using Patients-Derived Dermal Fibroblasts.Psychiatry investigation · 2025Article
- Fbxo16 mediates degradation of NF-κB p65 subunit and inhibits inflammatory response in dendritic cells.Frontiers in immunology · 2025Article
- ABLIM1: A novel oncogenic E3 ligase in colorectal cancer.Frontiers in oncology · 2025Article
- E3 ligase MKRN2 destabilizes PPP2CA proteins to inactivate canonical Wnt pathway and mitigates tumorigenesis of clear cell renal cell carcinoma.International journal of biological sciences · 2025Article
- WSB1/2 target chromatin-bound lysine-methylated RelA for proteasomal degradation and NF-κB termination.Nucleic acids research · 2024Article
- Early life exposure to vitamin D deficiency impairs molecular mechanisms that regulate liver cholesterol biosynthesis, energy metabolism, inflammation, and detoxification.Frontiers in endocrinology · 2024Article
- Dietary supplementation of nucleotides and oligosaccharides in kittens reduces the expression of circulating miR-1-3p, miR-133a-3p, miR-206-3p and miR-383-5p.Frontiers in veterinary science · 2024Article
- Identification and classification of papain-like cysteine proteinases.The Journal of biological chemistry · 2023Article
- Protective role of zinc in the pathogenesis of respiratory diseases.European journal of clinical nutrition · 2023Review
- The roles of E3 ubiquitin ligases in cancer progression and targeted therapy.Clinical and translational medicine · 2023Review
- MKRN2 knockout causes male infertility through decreasing STAT1, SIX4, and TNC expression.Frontiers in endocrinology · 2023Article
- MKRN1/2 serve as tumor suppressors in renal clear cell carcinoma by regulating the expression of p53.Cancer biomarkers : section A of Disease markers · 2023Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Activation of NF-κB transcription factor is strictly regulated to prevent excessive inflammatory responses leading to immunopathology. However, it still remains unclear how NF-κB activation is negatively controlled. The PDZ-LIM domain-containing protein PDLIM2 is a nuclear ubiquitin E3 ligase targeting the p65 subunit of NF-κB for degradation, thus terminating NF-κB-mediated inflammation. Using yeast two-hybrid screening, we sought to isolate PDLIM2-interacting proteins that are critical for suppressing NF-κB signaling. Here we identified MKRN2, a RING finger domain-containing protein that belongs to the makorin ring finger protein gene family, as a novel p65 ubiquitin E3 ligase. MKRN2 bound to p65 and promoted the polyubiquitination and proteasome-dependent degradation of p65 through the MKRN2 RING finger domain, thereby suppressing p65-mediated NF-κB transactivation. Notably, MKRN2 and PDLIM2 synergistically promote polyubiquitination and degradation of p65. Consistently, MKRN2 knockdown in dendritic cells resulted in larger amounts of nuclear p65 and augmented production of proinflammatory cytokines in responses to innate stimuli. These results delineate a novel role of MKRN2 in negatively regulating NF-κB-mediated inflammatory responses, cooperatively with PDLIM2.
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