title: Back to bases: how a nucleotide biosynthetic enzyme controls p53 activation.
abstract: In this issue, Reddy et al. (2014) reveal a new twist in the molecular mechanism leading to p53 activation upon cellular stress, illuminating an unexpected nuclear role for a nucleotide biosynthetic enzyme in regulation of a potent tumor suppressor.
authors: Howard Hughes Medical Institute and Department of Molecular, Cellular and Developmental Biology, University of Colorado at Boulder, Boulder, CO 80309, USA.
authors: Anna L
authors: AL
authors: Guarnieri
authors: Howard Hughes Medical Institute and Department of Molecular, Cellular and Developmental Biology, University of Colorado at Boulder, Boulder, CO 80309, USA. Electronic address: joaquin.espinosa@colorado.edu.
authors: Joaquín M
authors: JM
authors: Espinosa
mesh_terms: D000818:Animals; D019731:Carbon-Nitrogen Ligases / Q000502:physiology*; D005260:Female; D006801:Humans; D009711:Nucleotides / Q000096:biosynthesis*; D012261:Ribonucleoproteins / Q000502:physiology*; D016159:Tumor Suppressor Protein p53 / Q000378:metabolism*; D000099207:SS-A Antigen
chemical_list: D019731:Carbon-Nitrogen Ligases; D009711:Nucleotides; D012261:Ribonucleoproteins; D016159:Tumor Suppressor Protein p53; D000099207:SS-A Antigen; C020828:GMP synthase (glutamine-hydrolyzing)