Proteomics

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

ABSTRACT: 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., 2018, J. Biol. Chem 293(13): 4752-4766). Among them, we here choose 12 of the kinases to map the specific sites they phosphorylated on GPA1. In vitro kinase assays were preformed with 50 uM GDP in the reaction. Kinase # Locus No. 1 AT1G51800 2 AT4G33430 3 AT1G71830 4 AT1G72300 5 AT1G73080 6 AT3G13380 7 AT4G39400 8 AT5G49660 9 AT2G19230 10 AT2G37050 11 AT5G10290 12 AT5G62710

INSTRUMENT(S): Q Exactive Plus

ORGANISM(S): Arabidopsis Thaliana (ncbitaxon:3702)

SUBMITTER: Justin Walley  

PROVIDER: MSV000083963 | MassIVE | Wed Jun 12 13:29:00 BST 2019

REPOSITORIES: MassIVE

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Publications

Receptor-Like Kinase Phosphorylation of Arabidopsis Heterotrimeric G-Protein Gα -Subunit AtGPA1.

Jia Haiyan H   Song Gaoyuan G   Werth Emily G EG   Walley Justin W JW   Hicks Leslie M LM   Jones Alan M AM  

Proteomics 20191210 24

As molecular on-off switches, heterotrimeric G protein complexes, comprised of a Gα subunit and an obligate Gβγ dimer, transmit extracellular signals received by G protein-coupled receptors (GPCRs) to cytoplasmic targets that respond to biotic and abiotic stimuli. Signal transduction is modulated by phosphorylation of GPCRs and G protein complexes. In Arabidopsis thaliana, the Gα subunit AtGPA1 is phosphorylated by the receptor-like kinase (RLK) BRI1-associated Kinase 1 (BAK1), but the extent th  ...[more]

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