Phosphatidic Acid （PA） PP2A Activity and PIN1 Binds PP2AA1 to Regulate Polar Localization
Phospholipase D （PLD） exerts broad biological functions in eukaryotes through regulating downstream effectors by its product, phosphatidic acid （PA）. Protein kinases and phosphatases, such as mammalian target of rapa- mycin （mTOR）, Protein Phosphatase 1 （PP1） and Protein Phosphatase 2C （PP2C）, are P...
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| Published in | 分子植物：英文版 no. 5; pp. 1692 - 1702 |
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| Main Author | |
| Format | Journal Article |
| Language | English |
| Published |
2013
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| Subjects | |
| Online Access | Get full text |
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| Summary: | Phospholipase D （PLD） exerts broad biological functions in eukaryotes through regulating downstream effectors by its product, phosphatidic acid （PA）. Protein kinases and phosphatases, such as mammalian target of rapa- mycin （mTOR）, Protein Phosphatase 1 （PP1） and Protein Phosphatase 2C （PP2C）, are PA-binding proteins that execute crucial regulatory functions in both animals and plants. PA participates in many signaling pathways by modulating the enzymatic activity and/or subcellular localization of bound proteins. In this study, we demonstrated that PLD-derived PA interacts with the scaffolding A1 subunit of Protein Phosphatase 2A （PP2A） and regulates PP2A-mediated PIN1 dephos- phorylation in Arabidopsis. Genetic and pharmacological studies showed that both PA and PP2A participate in the regu- lation of auxin distribution. In addition, both the phosphorylation status and polar localization of PIN1 protein were affected by PLD inhibitors, Exogenous PA triggered the membrane accumulation of PP2AA1 and enhanced the PP2A activity at membrane, while PLD inhibition resulted in the reduced endosomal localization and perinuclear aggregation of PP2AA1. These results demonstrate the important role of PLD-derived PA in normal PP2A-mediated PIN dephosphoryl- ation and reveal a novel mechanism, in which PA recruits PP2AA1 to the membrane system and regulates PP2A function on membrane-targeted proteins. As PA and PP2A are conserved among eukaryotes, other organisms might use similar mechanisms to mediate multiple biological processes. |
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| Bibliography: | 31-2013/Q Phospholipase D （PLD） exerts broad biological functions in eukaryotes through regulating downstream effectors by its product, phosphatidic acid （PA）. Protein kinases and phosphatases, such as mammalian target of rapa- mycin （mTOR）, Protein Phosphatase 1 （PP1） and Protein Phosphatase 2C （PP2C）, are PA-binding proteins that execute crucial regulatory functions in both animals and plants. PA participates in many signaling pathways by modulating the enzymatic activity and/or subcellular localization of bound proteins. In this study, we demonstrated that PLD-derived PA interacts with the scaffolding A1 subunit of Protein Phosphatase 2A （PP2A） and regulates PP2A-mediated PIN1 dephos- phorylation in Arabidopsis. Genetic and pharmacological studies showed that both PA and PP2A participate in the regu- lation of auxin distribution. In addition, both the phosphorylation status and polar localization of PIN1 protein were affected by PLD inhibitors, Exogenous PA triggered the membrane accumulation of PP2AA1 and enhanced the PP2A activity at membrane, while PLD inhibition resulted in the reduced endosomal localization and perinuclear aggregation of PP2AA1. These results demonstrate the important role of PLD-derived PA in normal PP2A-mediated PIN dephosphoryl- ation and reveal a novel mechanism, in which PA recruits PP2AA1 to the membrane system and regulates PP2A function on membrane-targeted proteins. As PA and PP2A are conserved among eukaryotes, other organisms might use similar mechanisms to mediate multiple biological processes. phosphatidic acid （PA）; PP2A; PIN1 phosphorylation; polar localization. |
| ISSN: | 1674-2052 1752-9867 |