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CELL SIGNALING: Stat Acetylation--A Key Facet of Cytokine Signaling?
John J. O'Shea, Yuka Kanno, Xiaomin Chen, David E. Levy
Modification of proteins by addition of, for example, phosphate groups to particular amino acids in the protein is an important way to regulate the protein's activity. In their Perspective, O'Shea and colleagues discuss the intriguing finding that addition of an acetyl group to an amino acid in an important group of transcription factors called Stats might regulate their activity (Yuan et al.).
J. J. O'Shea and Y. Kanno are in the National Institute of Arthritis, Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, MD 20892, USA. X. Chen is in the Department of Biochemistry and Molecular Biology, University of Texas M. D. Anderson Cancer Center, Houston, TX 77030, USA. D. E. Levy is in the Departments of Pathology and Microbiology, New York University School of Medicine, New York, NY 10016, USA.
Lysine acetylation can generate highly charged enzymes with increased resistance toward irreversible inactivation.
B. F. Shaw, G. F. Schneider, B. Bilgicer, G. K. Kaufman, J. M. Neveu, W. S. Lane, J. P. Whitelegge, and G. M. Whitesides (2008)
Protein Sci.
17, 1446-1455
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