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Interaction of 14-3-3 with Signaling Proteins Is Mediated by the Recognition of Phosphoserine
Open accessAbstract
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.
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Metadata
- Authors
- Muslin, A. J., Tanner, J. W., Allen, P. M., & Shaw, A. S.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 1996-03
- Volume
- 84
- Issue
- 6
- Pages
- 889-897
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2024923170
- Cited by
- 1,381
- References
- 3
- FWCI
- 24.74
- Type
- journal article
- Language
- en
- Open access
- bronze
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