Post-translational modification of 14-3-3 isoforms and regulation of cellular function

Alastair Aitken

Research output: Contribution to journalArticlepeer-review

Abstract / Description of output

14-3-3 is now well established as a family of dimeric proteins that can modulate interaction between proteins involved in a wide range of functions. In many cases, these proteins show a distinct preference for a particular isoform(s) of 14-3-3 and in many cases a specific repertoire of dimer formation influences the particular proteins that 14-3-3 interact. Well over 200 proteins have been shown to interact with 14-3-3. The purpose of this review is to give an overview of the recently identified post-translational modifications of 14-3-3 isoforms and how this regulates function, interaction, specificity of dimerisation between isoforms and cellular location of target proteins. The association between 14-3-3 and its targets usually involves phosphorylation of the interacting protein which has been the subject of many reviews and discussion of this is included in other reviews in this series. However, it is now realised that in some cases the phosphorylation and a number of other, novel covalent modifications of 14-3-3 isoforms may modulate interaction and dimerisation of 14-3-3. Since this aspect is now emerging to be of major importance in the mechanism of regulation by 14-3-3 isoforms and has not been the focus of previous reviews, this will be detailed here.
Original languageEnglish
Pages (from-to)673-680
Number of pages8
JournalSeminars in Cell and Developmental Biology
Issue number7
Publication statusPublished - Sept 2011

Keywords / Materials (for Non-textual outputs)

  • 14-3-3
  • Isoforms
  • Post-translational modification
  • Phosphorylation
  • Protein–protein interaction


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