Literature DB >> 23974356

A bZIP protein, VIP1, interacts with Arabidopsis heterotrimeric G protein β subunit, AGB1.

Daisuke Tsugama1, Shenkui Liu, Tetsuo Takano.   

Abstract

Heterotrimeric G proteins (Gα, Gβ, Gγ) are signaling molecules conserved among eukaryotic species. The G proteins transmit signals via protein-protein interactions. By a yeast two-hybrid screen, we identified a bZIP protein, VIP1, as an Arabidopsis thaliana Gβ (AGB1)-interacting partner. The interaction between AGB1 and VIP1 was confirmed by an in vitro GST pull-down assay and a bimolecular fluorescence complementation (BiFC) assay. VIP1 was previously reported to be a regulator of osmosensory signaling. Interestingly, the BiFC pattern between AGB1 and VIP1 was speckled when cells were incubated in a hypotonic solution, but not when cells were incubated in a mannitol-containing hypertonic solution, suggesting that the subcellular localization of the AGB1-VIP1 complex is regulated by extracellular osmolarity and/or turgor pressure.
Copyright © 2013 Elsevier Masson SAS. All rights reserved.

Entities:  

Keywords:  ABA; AC; Arabidopsis thaliana; BiFC; G protein-coupled receptor; GAL4 DNA-binding domain; GAL4 activation domain; GAL4AD; GAL4BD; GPCR; Heterotrimeric G protein β subunit; NLS; Osmosensory signaling; PLC; Protein–protein interactions; RbcL; Rubisco large subunit; Transcription factor; Y2H; abscisic acid; adenylate cyclase; bimolecular fluorescence complementation; nuclear localization signal; phospholipase C; yeast two-hybrid

Mesh:

Substances:

Year:  2013        PMID: 23974356     DOI: 10.1016/j.plaphy.2013.07.024

Source DB:  PubMed          Journal:  Plant Physiol Biochem        ISSN: 0981-9428            Impact factor:   4.270


  10 in total

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  10 in total

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