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

Journal

PLANT MOLECULAR BIOLOGY
Volume 50, Issue 6, Pages 993-1010

Publisher

SPRINGER
DOI: 10.1023/A:1021261931561

Keywords

14-3-3; isoforms; signalling; phosphorylation; protein interaction motifs; regulation

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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.

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