title: Master of all things phosphorylated.
abstract: Serine/threonine phosphorylation plays a central role in cellular regulation, either by altering a protein's activity directly or by inducing specific protein-protein interactions, which, in turn, affect localization, binding specificity or activity. One group of molecules that bind to phosphoserine/phosphothreonine-containing sequences are the 14-3-3 proteins, which regulate a wide range of cellular targets. A new analysis of the 14-3-3 phosphoproteome using affinity chromatography has revealed many previously unknown 14-3-3 ligands whose binding to 14-3-3 proteins is phosphorylation-dependent. This study paves the way for future work on these important 14-3-3-interacting proteins.
authors.affiliation: Center for Cancer Research, Massachusetts Institute of Technology, 77 Massachusetts Avenue, E18-580, Cambridge, MA 02139, USA. myaffe@mit.edu
authors.forename: Michael B
authors.initials: MB
authors.lastname: Yaffe
mesh_terms: D048948:14-3-3 Proteins; D001665:Binding Sites; D002846:Chromatography, Affinity; D006801:Humans; D008024:Ligands; D010750:Phosphoproteins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D010766:Phosphorylation; D010768:Phosphoserine / Q000378:metabolism; D010769:Phosphothreonine / Q000378:metabolism; D014446:Tyrosine 3-Monooxygenase / Q000378:metabolism*
chemical_list: D048948:14-3-3 Proteins; D008024:Ligands; D010750:Phosphoproteins; D010769:Phosphothreonine; D010768:Phosphoserine; D014446:Tyrosine 3-Monooxygenase