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Proteomics. 2018 Dec;18(24):e1800323. doi: 10.1002/pmic.201800323.

Heterotrimeric G-Protein-Dependent Proteome and Phosphoproteome in Unstimulated Arabidopsis Roots.

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Department of Plant Pathology and Microbiology, Iowa State University, Ames, IA, USA.
Department of Biochemistry, Biophysics and Molecular Biology, Iowa State University, Ames, IA, USA.
Department of Biology and, Department of Pharmacology, University of North Carolina at Chapel Hill, Chapel Hill, NC, USA.


The G-protein complex is a cytoplasmic on-off molecular switch that is set by plasma membrane receptors that activate upon binding of its cognate extracellular agonist. In animals, the default setting is the "off" resting state, while in plants, the default state is constitutively "on" but repressed by a plasma membrane receptor-like protein. De-repression appears to involve specific phosphorylation of key elements of the G-protein complex and possibly target proteins that are positioned downstream of this complex. To address this possibility, protein abundance and phosphorylation state are quantified in wild type and G-protein deficient Arabidopsis roots in the unstimulated resting state. A total of 3246 phosphorylated and 8141 non-modified protein groups are identified. It has been found that 428 phosphorylation sites decrease and 509 sites increase in abundance in the G-protein quadrupole mutant lacking an operable G-protein-complex. Kinases with known roles in G-protein signaling including MAP KINASE 6 and FERONIA are differentially phosphorylated along with many other proteins now implicated in the control of G-protein signaling. Taken together, these datasets will enable the discovery of novel proteins and biological processes dependent on G-protein signaling.


G proteins; Tandem Mass Tags

[Available on 2019-12-01]
[Indexed for MEDLINE]

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