Dynamic interactions between 14-3-3 proteins and phosphoproteins regulate diverse cellular processes.
14-3-3 proteins exert an extraordinarily widespread influence on cellular processes in all eukaryotes. They operate by binding to specific phosphorylated sites on diverse target proteins, thereby forcing conformational changes or influencing interactions between their targets and other molecules. In these ways, 14-3-3s 'finish the job' when phosphorylation alone lacks the power to drive changes in the activities of intracellular proteins. By interacting dynamically with phosphorylated proteins, 14-3-3s often trigger events that promote cell survival--in situations from preventing metabolic imbalances caused by sudden darkness in leaves to mammalian cell-survival responses to growth factors. Recent work linking specific 14-3-3 isoforms to genetic disorders and cancers, and the cellular effects of 14-3-3 agonists and antagonists, indicate that the cellular complement of 14-3-3 proteins may integrate the specificity and strength of signalling through to different cellular responses.
Mackintosh
Carol
C
MRC Protein Phosphorylation Unit, School of Life Sciences, University of Dundee, Dundee DD1 5EH, Scotland, UK. c.mackintosh@dundee.ac.uk
D048948:14-3-3 Proteins / Q000737:chemistry / Q000378:metabolism*; D000818:Animals; D002468:Cell Physiological Phenomena; D006801:Humans; D010750:Phosphoproteins / Q000737:chemistry / Q000378:metabolism*; D025941:Protein Interaction Mapping; D020836:Protein Structure, Quaternary / Q000502:physiology
D048948:14-3-3 Proteins; D010750:Phosphoproteins