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Subcellular localization of VIP 1 is regulated by phosphorylation and 14‐3‐3 proteins
Author(s) -
Takeo Koichi,
Ito Takeshi
Publication year - 2017
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.12686
Subject(s) - dephosphorylation , phosphorylation , cytosol , subcellular localization , serine , transcription factor , microbiology and biotechnology , chemistry , leucine zipper , nuclear localization sequence , osmotic shock , biochemistry , arabidopsis , nuclear transport , nucleus , cell nucleus , biophysics , cytoplasm , phosphatase , biology , mutant , gene , enzyme
Arabidopsis basic leucine zipper transcription factor VIRE 2‐interacting protein 1 ( VIP 1) changes its localization from the cytosol to the nucleus when cells are subjected to mechanical or hypo‐osmotic stress, although the mechanism of this change is not known. In this study, we show that change in VIP 1 subcellular localization is synchronized with a change in the VIP 1 phosphorylation state that is induced by mechanical/hypo‐osmotic stress. VIP 1 has three phosphorylatable serine residues in HXRXXS motifs, which are 14‐3‐3‐binding targets. Mutations of these residues results in the lack of 14‐3‐3 binding and prevents cytosolic localization of VIP 1. These results suggest that dephosphorylation of VIP 1 resulting from mechanical or hypo‐osmotic stress induces nuclear localization via 14‐3‐3 dissociation.