Arabidopsis heterotrimeric G protein ¦Â subunit interacts with a plasma membrane 2C-type protein phosphatase, PP2C52

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• 作者：Daisuke Tsugama^a ; ^{tsugama@anesc.u-tokyo.ac.jp} ; Hua Liu^a ; ^{liuhua@anesc.u-tokyo.ac.jp} ; Shenkui Liu^b ; ^{shenkuiliu@nefu.edu.cn} ; Tetsuo Takano^a ; ^{takano@anesc.u-tokyo.ac.jp}
• 关键词：ABA ; abscisic acid ; BiFC ; bimolecular fluorescence complementation ; GPCR ; G protein-coupled receptor ; GST ; glutathione S-transferase ; ORF ; open reading frame ; PLC ; phospholipase C ; PP2C ; 2C-type protein phosphatase ; RT-PCR ; reverse transcription-PCR ; SE
• 刊名：Biochimica et Biophysica Acta (BBA)/Molecular Cell Research
• 出版年：2012
• 出版时间：December, 2012
• 年：2012
• 卷：1823
• 期：12
• 页码：2254-2260
• 全文大小：577 K

文摘

Heterotrimeric G proteins (G¦Á, G¦Â, G¦Ã) 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 G¦Â-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¦Â (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 dephosphorylation of other proteins.