Functional specificity in 14-3-3 isoform interactions through dimer formation and phosphorylation. Chromosome location of mammalian isoforms and variants.

Functional specificity in 14-3-3 isoform interactions through dimer formation and... 14-3-3 is now accepted as a novel type of dimeric protein that can modulate interaction between proteins involved in cell signalling and other functions. Target proteins that interact with 14-3-3 isoforms are involved in regulation of cell cycle, intracellular trafficking/targeting, signal transduction, cytoskeletal structure and transcription. In many cases, these proteins 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. The purpose of this review is to give an overview of mammalian 14-3-3 sequences, structures and post-translational modifications that may explain the known interactions with other proteins and mechanism(s). The regulation of interaction may involve phosphorylation of the interacting protein and in some cases the phosphorylation of 14-3-3 isoforms themselves. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Plant Molecular Biology Springer Journals

Functional specificity in 14-3-3 isoform interactions through dimer formation and phosphorylation. Chromosome location of mammalian isoforms and variants.

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Publisher
Kluwer Academic Publishers
Copyright
Copyright © 2002 by Kluwer Academic Publishers
Subject
Life Sciences; Biochemistry, general; Plant Sciences; Plant Pathology
ISSN
0167-4412
eISSN
1573-5028
D.O.I.
10.1023/A:1021261931561
Publisher site
See Article on Publisher Site

Abstract

14-3-3 is now accepted as a novel type of dimeric protein that can modulate interaction between proteins involved in cell signalling and other functions. Target proteins that interact with 14-3-3 isoforms are involved in regulation of cell cycle, intracellular trafficking/targeting, signal transduction, cytoskeletal structure and transcription. In many cases, these proteins 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. The purpose of this review is to give an overview of mammalian 14-3-3 sequences, structures and post-translational modifications that may explain the known interactions with other proteins and mechanism(s). The regulation of interaction may involve phosphorylation of the interacting protein and in some cases the phosphorylation of 14-3-3 isoforms themselves.

Journal

Plant Molecular BiologySpringer Journals

Published: Oct 13, 2004

References

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