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KMID : 0043320160390081075
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Archives of Pharmacal Research
2016 Volume.39 No. 8 p.1075 ~ p.1084
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Post-translational control of NF-κB signaling by ubiquitination
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Won Min-Ho
Byun Hee-Sun
Park Kyeong-Ah
Hur Gang-Min
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Abstract
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The transcription factor nuclear factor-kappa B (NF-κB) controls a number of essential cellular functions, including the immune response, cell proliferation, and apoptosis. NF-κB signaling must be engaged temporally and spatially and well orchestrated to prevent aberrant activation because loss of normal regulation of NF-κB is a major contributor to a variety of pathological diseases, including inflammatory diseases, autoimmune diseases, and cancers. Thus, understanding the molecular mechanisms controlling NF-κB activation is an important part of treatment of these relevant diseases. Although NF-κB transcriptional activity is largely regulated by nuclear translocation, post-translational modification of NF-κB signaling components, including phosphorylation, ubiquitination, acetylation, and methylation, has emerged as an important mechanism affecting activity. Many proteins have been shown to ubiquitinate and regulate NF-κB activation at the receptor signaling complex in response to a variety of ligands, such as tumor necrosis factor, interleukin-1, and Toll-like receptor ligands. In this review, we discuss our current knowledge of ubiquitination patterns and their functional role in NF-κB regulation.
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KEYWORD
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NF-κB, Ubiquitination, Post-translational modification, IKK, Receptor signaling complex
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