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Deubiquitination of NF-κB by Ubiquitin-Specific Protease-7 promotes transcription.

http://www.ncbi.nlm.nih.gov/pubmed/23267096

NF-κB is the master regulator of the immune response and is responsible for the transcription of hundreds of genes controlling inflammation and immunity. Activation of NF-κB occurs in the cytoplasm through the kinase activity of the IκB kinase complex, which leads to translocation of NF-κB to the nucleus. Once in the nucleus, NF-κB transcriptional activity is regulated by DNA binding-dependent ubiquitin-mediated proteasomal degradation. We have identified the deubiquitinase Ubiquitin Specific Protease-7 (USP7) as a regulator of NF-κB transcriptional activity. USP7 deubiquitination of NF-κB leads to increased transcription. Loss of USP7 activity results in increased ubiquitination of NF-κB, leading to reduced promoter occupancy and reduced expression of target genes in response to Toll-like- and TNF-receptor activation. These findings reveal a unique mechanism controlling NF-κB activity and demonstrate that the deubiquitination of NF-κB by USP7 is critical for target gene transcription.

Pubmed ID: 23267096 RIS Download

Mesh terms: Amino Acid Sequence | Animals | Cell Line, Tumor | Chromatin Immunoprecipitation | Gene Expression Regulation | HEK293 Cells | Humans | Immunoblotting | Immunoprecipitation | Mice | Models, Molecular | Molecular Sequence Data | NF-kappa B | NIH 3T3 Cells | Peptides | Real-Time Polymerase Chain Reaction | Transcription, Genetic | Transfection | Tumor Necrosis Factor-alpha | Ubiquitin Thiolesterase | Ubiquitination

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Associated grants

  • Agency: NIDDK NIH HHS, Id: R01 DK073639
  • Agency: NIDDK NIH HHS, Id: R01 DK073639

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