| Literature DB >> 23974356 |
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.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
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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