Proteomics

Dataset Information

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


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., 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.

INSTRUMENT(S): Q Exactive Plus

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

SUBMITTER: Justin Walley  

PROVIDER: MSV000083964 | MassIVE | Wed Jun 12 13:40:00 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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