title: Processive phosphorylation: mechanism and biological importance.
abstract: Recent proteomic data indicate that a majority of the phosphorylated proteins in a eucaryotic cell contain multiple sites of phosphorylation. In many signaling events, a single kinase phosphorylates multiple sites on a target protein. Processive phosphorylation occurs when a protein kinase binds once to a substrate and phosphorylates all of the available sites before dissociating. In this review, we discuss examples of processive phosphorylation by serine/threonine kinases and tyrosine kinases. We describe current experimental approaches for distinguishing processive from non-processive phosphorylation. Finally, we contrast the biological situations that are suited to regulation by processive and non-processive phosphorylation.
authors.affiliation: Department of Physiology and Biophysics, School of Medicine, Stony Brook University, Stony Brook, NY 11794, USA.
authors.forename: Parag
authors.initials: P
authors.lastname: Patwardhan
authors.forename: W Todd
authors.initials: WT
authors.lastname: Miller
mesh_terms: D000818:Animals; D050719:Crk-Associated Substrate Protein / Q000737:chemistry / Q000378:metabolism; D006801:Humans; D009687:Nuclear Proteins / Q000737:chemistry / Q000378:metabolism; D010766:Phosphorylation; D011499:Protein Processing, Post-Translational; D016601:RNA-Binding Proteins / Q000737:chemistry / Q000378:metabolism; D000068103:Serine-Arginine Splicing Factors
chemical_list: D050719:Crk-Associated Substrate Protein; D009687:Nuclear Proteins; D016601:RNA-Binding Proteins; D000068103:Serine-Arginine Splicing Factors