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

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Song, Gaoyuan
Brachova, Libuse
Jones, Alan M.
Walley, Justin W.
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© 2018 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Nikolau, Basil
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Plant Pathology and Microbiology
The Department of Plant Pathology and Microbiology and the Department of Entomology officially merged as of September 1, 2022. The new department is known as the Department of Plant Pathology, Entomology, and Microbiology (PPEM). The overall mission of the Department is to benefit society through research, teaching, and extension activities that improve pest management and prevent disease. Collectively, the Department consists of about 100 faculty, staff, and students who are engaged in research, teaching, and extension activities that are central to the mission of the College of Agriculture and Life Sciences. The Department possesses state-of-the-art research and teaching facilities in the Advanced Research and Teaching Building and in Science II. In addition, research and extension activities are performed off-campus at the Field Extension Education Laboratory, the Horticulture Station, the Agriculture Engineering/Agronomy Farm, and several Research and Demonstration Farms located around the state. Furthermore, the Department houses the Plant and Insect Diagnostic Clinic, the Iowa Soybean Research Center, the Insect Zoo, and BugGuide. Several USDA-ARS scientists are also affiliated with the Department.
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Plant Pathology and MicrobiologyBiochemistry, Biophysics and Molecular Biology
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.
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.