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- W1973312670 endingPage "680" @default.
- W1973312670 startingPage "673" @default.
- W1973312670 abstract "► Dimeric 14-3-3 isoforms modulate protein interactions in a wide range of functions. ► 14-3-3s interact with over 200 protein kinases, phosphatases and other signalling proteins. ► Association usually involves phosphorylation of the interactor on novel phosphoserine motifs. ► Phosphorylation and other modifications of 14-3-3 itself may also modulate interaction. ► Acetylation of lysines or acylation of both 14-3-3 and its targets can also affect interaction. 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." @default.
- W1973312670 created "2016-06-24" @default.
- W1973312670 creator A5053808626 @default.
- W1973312670 date "2011-09-01" @default.
- W1973312670 modified "2023-10-06" @default.
- W1973312670 title "Post-translational modification of 14-3-3 isoforms and regulation of cellular function" @default.
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