title: 14-3-3 proteins: a number of functions for a numbered protein.
abstract: Many signal transduction events are orchestrated by specific interactions of proteins mediated through discrete phosphopeptide-binding motifs. Although several phosphospecific-binding domains are now known, 14-3-3s were the first proteins recognized to specifically bind a discrete phosphoserine or phosphothreonine motif. The 14-3-3 proteins are a family of ubiquitously expressed, exclusively eukaryotic proteins with an astonishingly large number of binding partners. Consequently, 14-3-3s modulate an enormous and diverse group of cellular processes. The effects of 14-3-3 proteins on their targets can be broadly defined using three categories: (i) conformational change; (ii) physical occlusion of sequence-specific or structural protein features; and (iii) scaffolding. This review will describe the current state of knowledge on 14-3-3 proteins, highlighting several important advances, and will attempt to provide a framework by which 14-3-3 functions can be understood.
authors.affiliation: Department of Biological Sciences, University of Calgary, 2500 University Drive N.W., Calgary, Canada AB T2N 1N4.
authors.forename: Dave
authors.initials: D
authors.lastname: Bridges
authors.forename: Greg B G
authors.initials: GB
authors.lastname: Moorhead
mesh_terms: D048948:14-3-3 Proteins; D000595:Amino Acid Sequence; D000818:Animals; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D014446:Tyrosine 3-Monooxygenase / Q000502:physiology*
chemical_list: D048948:14-3-3 Proteins; D014446:Tyrosine 3-Monooxygenase