Structure and sites of phosphorylation of 14-3-3 protein: role in coordinating signal transduction pathways

The 14-3-3 family are homo- and heterodimeric proteins whose biological role has been unclear for some time, although they are now gaining acceptance as a novel type of 'adaptor' protein that modulates interactions between components of signal transduction pathways, rather than by direct a...

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Bibliographic Details
Published in:Journal of Protein Chemistry 1997-07, Vol.16 (5), p.513-522
Main Authors: Dubois, T, Howell, S, Amess, B, Kerai, P, Learmonth, M, Madrazo, J, Chaudhri, M, Rittinger, K, Scarabel, M, Soneji, Y, Aitken, A
Format: Article
Language:English
Subjects:
14-3-3 protein
14-3-3 Proteins
Adaptor proteins
Amino Acid Sequence
Animals
Binding Sites
Brain - enzymology
Conserved sequence
Crystal structure
Enzyme Inhibitors - metabolism
Fungal Proteins - metabolism
Fungal Proteins - physiology
Isoforms
Isomerism
Kinases
Molecular biology
Molecular Sequence Data
Pathways
Phosphorylation
Phosphoserine
Protein Conformation
Protein Kinase C - metabolism
Protein Structure, Tertiary
Proteins
Proteins - metabolism
Proteins - physiology
Raf protein
Saccharomyces cerevisiae - metabolism
Saccharomyces cerevisiae - physiology
Sequence Homology, Amino Acid
Signal transduction
Signal Transduction - physiology
Structure-Activity Relationship
Swine
Tyrosine 3-Monooxygenase
Yeasts
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Summary:The 14-3-3 family are homo- and heterodimeric proteins whose biological role has been unclear for some time, although they are now gaining acceptance as a novel type of 'adaptor' protein that modulates interactions between components of signal transduction pathways, rather than by direct activation or inhibition. It is becoming apparent that phosphorylation of the binding partner and possibly also the 14-3-3 proteins may regulate these interactions. 14-3-3 isoforms interact with a novel phosphoserine (Sp) motif on many proteins, RSX1,2SpXP. The two isoforms that interact with Raf-1 are phosphorylated in vivo on Ser185 in a consensus sequence motif for proline-directed kinases. The crystal structure of 14-3-3 indicates that this phosphorylation could regulate interaction of 14-3-3 with its target proteins. We have now identified a number of additional phosphorylation sites on distinct mammalian and yeast isoforms.
ISSN:0277-8033
1572-3887
1573-4943
DOI:10.1023/A:1026321813463