Interaction of 14-3-3 with signaling proteins is mediated by the recognition of phosphoserine

A. J. Muslin, J. W. Tanner, P. M. Allen, A. S. Shaw

Research output: Contribution to journalArticlepeer-review

1104 Scopus citations

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.

Original languageEnglish
Pages (from-to)889-897
Number of pages9
JournalCell
Volume84
Issue number6
DOIs
StatePublished - Jan 1 1996
Externally publishedYes

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