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Molecular & Cellular Proteomics 8:1167-1173, 2009.
© 2009 by The American Society for Biochemistry and Molecular Biology, Inc.

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Research

Identification of New p53 Acetylation Sites in COS-1 Cells^*

Anita Joubel, Robert J. Chalkley, Katalin F. Medzihradszky, Hubert Hondermarck and Alma L. Burlingame^,¶

From the Department of Pharmaceutical Chemistry, University of California, San Francisco, California 94158-2517 and
INSERM U 908, "Growth factor signaling in breast cancer. Functional proteomics," University Lille 1, 59655 Villeneuve d'Ascq, France

The p53 tumor suppressor protein is a key regulator of cell cycle and death that is involved in many cell signaling pathways and is tightly regulated in mammalian cells. Post-translational modifications of p53 have been investigated previously mainly using antibodies. In this study, utilizing LC-MS/MS analysis, we have characterized p53 protein from COS-1 cells. Several already known post-translational modifications were observed, such as phosphorylation on serines 15, 33, 315, and 392 as well as acetylation on lysines 305, 370, 372, 373, 381, 382, and 386. Interestingly novel acetylation sites were identified at lysines 319 and 357. This study confirmed that p53 is a highly acetylated protein and revealed new acetylation sites that might aid the further understanding of p53 regulation.

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				D. W. Meek and C. W. Anderson Posttranslational Modification of p53: Cooperative Integrators of Function Cold Spring Harb Perspect Biol, December 1, 2009; 1(6): a000950 - a000950. [Abstract] [Full Text] [PDF]