Functional specificity in 14-3-3 isoform interactions through dimer formation and phosphorylation. Chromosome location of mammalian isoforms and variants.
14-3-3 is now accepted as a novel type of dimeric protein that can modulate interaction between proteins involved in cell signalling and other functions. Target proteins that interact with 14-3-3 isoforms are involved in regulation of cell cycle, intracellular trafficking/targeting, signal transduction, cytoskeletal structure and transcription. In many cases, these proteins show a distinct preference for a particular isoform(s) of 14-3-3. A specific repertoire of dimer formation may influence which of the 14-3-3 interacting proteins could be brought together. The purpose of this review is to give an overview of mammalian 14-3-3 sequences, structures and post-translational modifications that may explain the known interactions with other proteins and mechanism(s). The regulation of interaction may involve phosphorylation of the interacting protein and in some cases the phosphorylation of 14-3-3 isoforms themselves.
Aitken
Alastair
A
University of Edinburgh, Division of Biomedical and Clinical Laboratory Sciences, Hugh Robson Building, George Square, Edinburgh, EH8 9XD Scotland, UK. Alastair.Aitken@ed.ac.uk
D048948:14-3-3 Proteins; D000595:Amino Acid Sequence; D000818:Animals; D002874:Chromosome Mapping; D019281:Dimerization; D014644:Genetic Variation; D006801:Humans; D008969:Molecular Sequence Data; D010766:Phosphorylation; D011485:Protein Binding; D020033:Protein Isoforms / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D017434:Protein Structure, Tertiary; D015398:Signal Transduction / Q000502:physiology*; D013045:Species Specificity; D014446:Tyrosine 3-Monooxygenase / Q000235:genetics / Q000378:metabolism* / Q000502:physiology
D048948:14-3-3 Proteins; D020033:Protein Isoforms; D014446:Tyrosine 3-Monooxygenase