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- Brian Skaug
- Department of Molecular Biology, University of Texas Southwestern Medical Center, Dallas, Texas 75390-9148;
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- Xiaomo Jiang
- Department of Molecular Biology, University of Texas Southwestern Medical Center, Dallas, Texas 75390-9148;
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- Zhijian J. Chen
- Department of Molecular Biology, University of Texas Southwestern Medical Center, Dallas, Texas 75390-9148;
書誌事項
- 公開日
- 2009-06-01
- DOI
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- 10.1146/annurev.biochem.78.070907.102750
- 公開者
- Annual Reviews
この論文をさがす
説明
<jats:p> Nuclear factor kappa enhancer binding protein (NF-κB) regulates diverse biological processes including immunity, inflammation, and apoptosis. A vast array of cellular stimuli converges on NF-κB, and ubiquitination plays an essential role in the coordination of these signals to regulate NF-κB activity. At least three steps in NF-κB activation directly involve ubiquitination: proteasomal degradation of inhibitor of NF-κB (IκB), processing of NF-κB precursors, and activation of the transforming growth factor (TGF)-β-activated kinase (TAK1) and IκB kinase (IKK) complexes. In this review, we discuss recent advances in the identification and characterization of ubiquitination and deubiquitination machinery that regulate NF-κB. Particular emphasis is given to proteasome-independent functions of ubiquitin, specifically its role in the activation of protein kinase complexes and in coordination of cell survival and apoptosis signals downstream of tumor necrosis factor α (TNFα). </jats:p>
収録刊行物
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- Annual Review of Biochemistry
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Annual Review of Biochemistry 78 (1), 769-796, 2009-06-01
Annual Reviews