14-3-3s are evolutionarily conserved eukaryotic regulatory proteins that are involved in diverse biological processes. The common mode of action for the 14-3-3 proteins is through the binding of phosphorylated target proteins. In many species, multiple 14-3-3 isoforms exist and these different isoforms can exhibit distinct ranges of target interactions. The dimerization of 14-3-3s is central to their function. 14-3-3 isoforms can form different combinations of homo- and heterodimers, which contribute to the broad functional diversity of the family. In this study, we showed that phosphomimetic mutation of a conserved serine residue in the dimerization interface of 14-3-3 isoforms, Ser-62, not only affects the ability of Arabidopsis 14-3-3ω to form homodimers, but alters the range of 14-3-3 family members with which it can form heterodimers. Furthermore, we demonstrated that the phosphorylation status of Ser-62 can regulate the binding of 14-3-3ω to target proteins, suggesting that Ser-62 might be a conserved key element to modulate target binding in both plants and animals.

• PMID: 26512969
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Journal Article | Research Support, U.S. Gov't, Non-P.H.S.

Authors

Gökirmak T, Denison FC, Laughner BJ, Paul AL, Ferl RJ

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