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.
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August 2002
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Conference Article|
August 01 2002
Specificity of 14-3-3 isoform dimer interactions and phosphorylation
A. Aitken;
A. Aitken
1
1University of Edinburgh, Division of Biomedical and Clinical Laboratory Sciences, Hugh Robson Building, George Square, Edinburgh EH8 9XD, Scotland, U.K.
1To whom correspondence should be addressed (e-mail Alastair.Aitken@ed.ac.uk)
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H. Baxter;
H. Baxter
1University of Edinburgh, Division of Biomedical and Clinical Laboratory Sciences, Hugh Robson Building, George Square, Edinburgh EH8 9XD, Scotland, U.K.
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T. Dubois;
T. Dubois
1University of Edinburgh, Division of Biomedical and Clinical Laboratory Sciences, Hugh Robson Building, George Square, Edinburgh EH8 9XD, Scotland, U.K.
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S. Clokie;
S. Clokie
1University of Edinburgh, Division of Biomedical and Clinical Laboratory Sciences, Hugh Robson Building, George Square, Edinburgh EH8 9XD, Scotland, U.K.
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S. Mackie;
S. Mackie
1University of Edinburgh, Division of Biomedical and Clinical Laboratory Sciences, Hugh Robson Building, George Square, Edinburgh EH8 9XD, Scotland, U.K.
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K. Mitchell;
K. Mitchell
1University of Edinburgh, Division of Biomedical and Clinical Laboratory Sciences, Hugh Robson Building, George Square, Edinburgh EH8 9XD, Scotland, U.K.
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A. Peden;
A. Peden
1University of Edinburgh, Division of Biomedical and Clinical Laboratory Sciences, Hugh Robson Building, George Square, Edinburgh EH8 9XD, Scotland, U.K.
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E. Zemlickova
E. Zemlickova
1University of Edinburgh, Division of Biomedical and Clinical Laboratory Sciences, Hugh Robson Building, George Square, Edinburgh EH8 9XD, Scotland, U.K.
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Publisher: Portland Press Ltd
Received:
April 10 2002
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© 2002 Biochemical Society
2002
Biochem Soc Trans (2002) 30 (4): 351–360.
Article history
Received:
April 10 2002
Citation
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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