The project intended to reveal protein phosphorylation patterns in Arabidopsis thaliana in response to ATP. For this purpose, Arabidopsis thaliana plants, including WT, ATP receptor mutants (p2k1, p2k2, and double mutant p2k1/p2k2), and P2K1 overexpression plants, were treated with ATP or buffer (as the negative control). Crude membrane proteins were then extracted, reduced with DTT, alkylated with iodoacetamide, and digested with Lys-C/trypsin. The digested peptides were then acidified with formic acid, desalted with C18 SPE columns, and concentrated in a Speed-Vac concentrator. The Phosphopeptides were enriched from the above digested peptide samples using IMAC and then analyzed with LC-MS/MS. Data was searched with MaxQuant (ver. 2.0.1.0), which identified and quantified peptides and proteins across all of with Arabidopsis thaliana data set (Uniprot.2020.11.02).
[doi:10.25345/C5BN9XF2J]
[dataset license: CC0 1.0 Universal (CC0 1.0)]
Keywords: phosphorylation ; ATP
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Principal Investigators: (in alphabetical order) |
Gary Stacey, University of Missouri, Columbia, United States |
| Submitting User: | alchemistmatt |
Kim D, Jorge GL, Xu C, Su L, Cho SH, Ahsan N, Chen D, Zhou L, Gritsenko MA, Zhou M, Wan J, Pasa-Tolic L, Xu D, Bartley LE, Thelen JJ, Stacey G.
Identifying receptor kinase substrates using an 8,000 peptide kinase client library enriched for conserved phosphorylation sites.
Mol Cell Proteomics. Epub 2025 Feb 7.
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