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XB-ART-18413
Cell 1996 Mar 22;846:889-97. doi: 10.1016/s0092-8674(00)81067-3.
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Interaction of 14-3-3 with signaling proteins is mediated by the recognition of phosphoserine.

Muslin AJ , Tanner JW , Allen PM , Shaw AS .


Abstract
The highly conserved and ubiquitously expressed 14-3-3 family of proteins bind to a variety of proteins involved in signal transduction and cell cycle regulation. The nature and specificity of 14-3-3 binding is, however, not known. Here we show that 14-3-3 is a specific phosphoserine-binding protein. Using a panel of phosphorylated peptides based on Raf-1, we have defined the 14-3-3 binding motif and show that most of the known 14-3-3 binding proteins contain the motif. Peptides containing the motif could disrupt 14-3-3 complexes and inhibit maturation of Xenopus laevis oocytes. These results suggest that the interactions of 14-3-3 with signaling proteins are critical for the activation of signaling proteins. Our findings also suggest novel roles for serine/threonine phosphorylation in the assembly of protein-protein complexes.

PubMed ID: 8601312
Article link: Cell
Grant support: [+]