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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.

Original publication

DOI

10.1023/a:1026321813463

Type

Conference paper

Publication Date

07/1997

Volume

16

Pages

513 - 522

Addresses

National Institute for Medical Research, London, United Kingdom.

Keywords

Brain, Animals, Swine, Saccharomyces cerevisiae, Tyrosine 3-Monooxygenase, Protein Kinase C, 14-3-3 Proteins, Proteins, Fungal Proteins, Enzyme Inhibitors, Signal Transduction, Binding Sites, Amino Acid Sequence, Protein Conformation, Protein Structure, Tertiary, Sequence Homology, Amino Acid, Structure-Activity Relationship, Phosphorylation, Isomerism, Molecular Sequence Data