Abstract
Posttranslational modifications of NF-κB, including phosphorylation, acetylation, and methylation, have emerged as important regulatory mechanisms to control the transcriptional outcomes of this important transcription factor. These modifications work independently, sequentially or in combination to modulate the diverse biological functions of NF-κB in cancer and inflammatory response. Here, we describe some experimental methods to detect the in vitro and in vivo phosphorylation and acetylation of NF-κB, specifically focusing on the RelA subunit of NF-κB. These methods include labeling the phospho- or acetyl- groups with radioisotopes in vitro and immunoblotting with site-specific anti-phospho-serine or acetyl-lysine antibodies in culture cells and tissue samples.
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Acknowledgments
The work described in this article was supported in part by funds from University of Illinois at Urbana-Champaign.
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Modi, N.T., Chen, LF. (2021). Measuring NF-κB Phosphorylation and Acetylation. In: Franzoso, G., Zazzeroni, F. (eds) NF-κB Transcription Factors. Methods in Molecular Biology, vol 2366. Humana, New York, NY. https://doi.org/10.1007/978-1-0716-1669-7_1
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DOI: https://doi.org/10.1007/978-1-0716-1669-7_1
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