Journal article
Physical Interaction with Yes-associated Protein Enhances p73 Transcriptional Activity*
Abstract
Specific protein-protein interactions are involved in a large number of cellular processes and are mainly mediated by structurally and functionally defined domains. Here we report that the nuclear phosphoprotein p73 can engage in a physical association with the Yes-associated protein (YAP). This association occurs under physiological conditions as shown by reciprocal co-immunoprecipitation of complexes from lysates of P19 cells. The WW domain …
Authors
Strano S; Munarriz E; Rossi M; Castagnoli L; Shaul Y; Sacchi A; Oren M; Sudol M; Cesareni G; Blandino G
Journal
Journal of Biological Chemistry, Vol. 276, No. 18, pp. 15164–15173
Publisher
Elsevier
Publication Date
1 2001
DOI
10.1074/jbc.m010484200
ISSN
0021-9258
Associated Experts
Fields of Research (FoR)
Medical Subject Headings (MeSH)
Adaptor Proteins, Signal TransducingAmino Acid SequenceBase SequenceCarrier ProteinsCell LineDNA PrimersDNA-Binding ProteinsFluorescent Antibody Technique, IndirectGenes, Tumor SuppressorGreen Fluorescent ProteinsHumansLuminescent ProteinsMolecular Sequence DataNuclear ProteinsPhosphoproteinsPoint MutationProtein BindingRecombinant Fusion ProteinsSignal TransductionTranscription FactorsTranscription, GeneticTumor Protein p73Tumor Suppressor ProteinsYAP-Signaling Proteins