Subcellular localization of VIP1 is regulated by phosphorylation and 14-3-3 proteins

FEBS Lett. 2017 Jul;591(13):1972-1981. doi: 10.1002/1873-3468.12686. Epub 2017 Jun 22.

Abstract

Arabidopsis basic leucine zipper transcription factor VIRE2-interacting protein 1 (VIP1) 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 VIP1 subcellular localization is synchronized with a change in the VIP1 phosphorylation state that is induced by mechanical/hypo-osmotic stress. VIP1 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 VIP1. These results suggest that dephosphorylation of VIP1 resulting from mechanical or hypo-osmotic stress induces nuclear localization via 14-3-3 dissociation.

Keywords: dephosphorylation; hypo-osmotic stress; mechanical stress.

Publication types

  • Letter

MeSH terms

  • 14-3-3 Proteins / metabolism*
  • Active Transport, Cell Nucleus
  • Amino Acid Sequence
  • Arabidopsis / cytology
  • Arabidopsis / metabolism
  • Arabidopsis Proteins / metabolism*
  • Biomechanical Phenomena
  • Cell Nucleus / metabolism
  • Cytoplasm / metabolism
  • Intracellular Space / metabolism*
  • Osmotic Pressure
  • Phosphorylation
  • Protein Transport
  • Serine / metabolism
  • Signal Transduction

Substances

  • 14-3-3 Proteins
  • Arabidopsis Proteins
  • VIP1 protein, Arabidopsis
  • Serine