title: Regulation of p53 function by lysine methylation.
abstract: The reversible and dynamic methylation of proteins on lysine residues can greatly increase the signaling potential of the modified factor. In addition to histones, several other nuclear factors such as the tumor suppressor and transcription factor p53 undergo lysine methylation, suggesting that this modification may be a common mechanism for modulating protein–protein interactions and key cellular signaling pathways. This article focuses on how lysine methylation events on the C-terminal tail of p53 are generated, sensed and transduced to modulate p53 functions.
authors.affiliation: Department of Biology, Stanford University, Stanford, CA 94305, USA.
authors.forename: Lisandra E
authors.initials: LE
authors.lastname: West
authors.forename: Or
authors.initials: O
authors.lastname: Gozani
mesh_terms: D044127:Epigenesis, Genetic / Q000502:physiology*; D006649:Histocompatibility Antigens / Q000378:metabolism; D056466:Histone Demethylases / Q000378:metabolism; D011495:Histone-Lysine N-Methyltransferase / Q000378:metabolism; D006657:Histones / Q000378:metabolism; D006801:Humans; D008239:Lysine / Q000378:metabolism*; D008745:Methylation; D008954:Models, Biological; D015398:Signal Transduction / Q000502:physiology*; D016159:Tumor Suppressor Protein p53 / Q000378:metabolism*
chemical_list: D006649:Histocompatibility Antigens; D006657:Histones; D016159:Tumor Suppressor Protein p53; D056466:Histone Demethylases; C495195:KDM1A protein, human; C445405:EHMT2 protein, human; D011495:Histone-Lysine N-Methyltransferase; C540312:SETD7 protein, human; C512569:SMYD2 protein, human; D008239:Lysine