MassIVE MSV000083964

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Identification of the Kinase phosphorylation sites on AtGPA1 in presence of GTP

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Description

Phosphorylation of GPA1 has been shown to functionally important in vitro and in vivo. We previously identified18 LRR RLKs transphosphorylation of AtGPA1 via in vitro kinase assay using recombinant kinase domains and AtGPA1 (Bo et al., J Biol Chem 293(13): 4752-4766). Among them, we choose 12 kinases to identify the specific sites they phosphorylated on atGPA1 by mass spec analysis. In vitro kinase reactions were performed in the presence of GTP. [doi:10.25345/C5BH15] [dataset license: CC0 1.0 Universal (CC0 1.0)]

Keywords: G Protein ; GTP ; In vitro kinase

Contact

Principal Investigators:
(in alphabetical order) 		Justin Walley, Iowa State University, US
Submitting User: jwalley

Publications

Jia H, Song G, Werth EG, Walley JW, Hicks LM, Jones AM.
Receptor-Like Kinase Phosphorylation of Arabidopsis Heterotrimeric G-Protein G? -Subunit AtGPA1.
Proteomics. 2019 Dec;19(24):e1900265. Epub 2019 Dec 10.

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