title: Structurally constrained residues outside the binding motif are essential in the interaction of 14-3-3 and phosphorylated partner.
abstract: 14-3-3 proteins participate in many key cellular processes after binding to disordered phospho-partners. Usually, the phosphorylated state is an essential target for the binding. Here, we show for the first time residues other than those in the 14-3-3 binding motif that are essential for the binding between 14-3-3 and a phosphorylated partner. Results support that phosphorylation, although necessary, is not sufficient for 14-3-3's complex formation, as structurally constrained anchor residues play a critical function in stabilizing the protein-protein interaction.
authors.affiliation: Instituto Tecnológico de Chascomús (IIB-INTECH, CONICET-UNSAM), Camino Circunvalación Laguna, Km 6 cc164, Chascomus B7130IWA, Argentina.
authors.forename: Marina
authors.initials: M
authors.lastname: Uhart
authors.forename: Alberto A
authors.initials: AA
authors.lastname: Iglesias
authors.forename: Diego M
authors.initials: DM
authors.lastname: Bustos
mesh_terms: D048948:14-3-3 Proteins / Q000737:chemistry* / Q000378:metabolism*; D000818:Animals; D047068:Arylalkylamine N-Acetyltransferase / Q000737:chemistry* / Q000378:metabolism*; D001665:Binding Sites; D007700:Kinetics; D008958:Models, Molecular; D010766:Phosphorylation; D011485:Protein Binding; D025941:Protein Interaction Mapping; D012756:Sheep
chemical_list: D048948:14-3-3 Proteins; D047068:Arylalkylamine N-Acetyltransferase