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Cited by 1,381

The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.

Interaction of 14-3-3 with Signaling Proteins Is Mediated by the Recognition of Phosphoserine

Open access
Muslin, Anthony J, Tanner, J.William, Allen, Paul M, Shaw, Andrey S·1996·Cell

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.

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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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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

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