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

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2018-12
Authors
Song, Gaoyuan
Brachova, Libuse
Nikolau, Basil
Jones, Alan M.
Walley, Justin W.
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© 2018 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
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Plant Pathology and MicrobiologyBiochemistry, Biophysics and Molecular Biology
Abstract
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, we quantified protein abundance and phosphorylation state in wild type and G-protein deficient Arabidopsis roots in the unstimulated resting state. A total of 3,246 phosphorylated and 8,141 non-modified protein groups were identified. We found that 428 phosphorylation sites decreased and 509 sites increased 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 were 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.
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This is the peer reviewed version of the following article: Song, Gaoyuan, Libuse Brachova, Basil J. Nikolau, Alan M. Jones, and Justin W. Walley. "Heterotrimeric G‐Protein‐Dependent Proteome and Phosphoproteome in Unstimulated Arabidopsis Roots." Proteomics 18, no. 24 (2018): 1800323, which has been published in final form at DOI:10.1002/pmic.201800323. This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Use of Self-Archived Versions. This article may not be enhanced, enriched or otherwise transformed into a derivative work, without express permission from Wiley or by statutory rights under applicable legislation. Copyright notices must not be removed, obscured or modified. The article must be linked to Wiley’s version of record on Wiley Online Library and any embedding, framing or otherwise making available the article or pages thereof by third parties from platforms, services and websites other than Wiley Online Library must be prohibited.
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