Proteins that interact with 14-3-3 isoforms are involved in regulation of the cell cycle, intracellular trafficking/targeting, signal transduction, cytoskeletal structure and transcription. Recent novel roles for 14-3-3 isoforms include nuclear trafficking the direct interaction with cruciform DNA and with a number of receptors, small G-proteins and their regulators. Recent findings also show that the mechanism of interaction is also more complex than the initial finding of the novel phosphoserine/threonine motif. Non-phosphorylated binding motifs that can also be of high affinity may show a more isoform-dependent interaction and binding of a protein through two distinct binding motifs to a dimeric 14-3-3 may also be essential for full interaction. Phosphorylation of specific 14-3-3 isoforms can also regulate interactions. In many cases, they show a distinct preference for a particular isoform(s) of 14-3-3. A specific repertoire of dimer formation may influence which of the 14-3-3-interacting proteins could be brought together. Mammalian and yeast 14-3-3 isoforms show a preference for dimerization with specific partners in vivo.
Specificity of 14-3-3 isoform dimer interactions and phosphorylation
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A. Aitken, H. Baxter, T. Dubois, S. Clokie, S. Mackie, K. Mitchell, A. Peden, E. Zemlickova; Specificity of 14-3-3 isoform dimer interactions and phosphorylation. Biochem Soc Trans 1 August 2002; 30 (4): 351–360. doi: https://doi.org/10.1042/bst0300351
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