Identification of new p53 acetylation sites in COS-1 cells.
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.
Joubel
Anita
A
Department of Pharmaceutical Chemistry, University of California, San Francisco, California 94158-2517, USA.
Chalkley
Robert J
RJ
Medzihradszky
Katalin F
KF
Hondermarck
Hubert
H
Burlingame
Alma L
AL
D000107:Acetylation; D000595:Amino Acid Sequence; D000818:Animals; D019556:COS Cells; D002522:Chlorocebus aethiops; D002853:Chromatography, Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D008969:Molecular Sequence Data; D011499:Protein Processing, Post-Translational; D053719:Tandem Mass Spectrometry; D016159:Tumor Suppressor Protein p53 / Q000737:chemistry / Q000378:metabolism*
D016159:Tumor Suppressor Protein p53