Journal
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH
Volume 1823, Issue 12, Pages 2254-2260Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbamcr.2012.10.001
Keywords
Abscisic acid; Arabidopsis; Heterotrimeric G protein 13 subunit; Myristoylation; PP2C; Protein-protein interaction
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Funding
- RIKEN BRC [21380002, 22.2144, RAFL05-19-B08, RAFL22-41-E11, RAFL18-04-O14]
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HeterotrimericG proteins (G alpha, G beta, G gamma) play important roles in signal transduction among various eukaryotic species. G proteins transmit signals by regulating the activities of effector proteins, but only a few GO-interacting effectors have been identified in plants. Here we show by a yeast two-hybrid screen that a putative myristoylated 2C-type protein phosphatase, PP2C52, is an Arabidopsis G beta (AGB1)-interacting partner. The interaction between AGB1 and PP2C52 was confirmed by an in vitro pull-down assay and a bimolecular fluorescence complementation assay. PP2C52 transcripts were detected in many tissues. PP2C52 was localized to the plasma membrane and a mutation in the putative myristoylation site of PP2C52 disrupted its plasma membrane localization. Our results suggest that PP2C52 interacts with AGB1 on the plasma membrane and transmits signals via dephosphotylation of other proteins. (C) 2012 Elsevier B.V. All rights reserved.
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