Binding of phosphatidic acid to 14-3-3 proteins hampers their ability to activate the plant plasma membrane H(+) -ATPase
| Autor: | Lorenzo Camoni, Roberta Pallucca, Patrizia Aducci, Cristina Di Lucente, Sabina Visconti |
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| Jazyk: | angličtina |
| Rok vydání: | 2012 |
| Předmět: |
Settore BIO/04
G protein ATPase Clinical Biochemistry Phosphatidic Acids Plasma protein binding Biochemistry Zea mays Cell membrane chemistry.chemical_compound Stress Physiological Catalytic Domain Genetics medicine Phospholipase D Phosphorylation Molecular Biology Plant Proteins biology PLD2 Cell Membrane Cell Biology Phosphatidic acid Cell biology Enzyme Activation Proton-Translocating ATPases medicine.anatomical_structure chemistry 14-3-3 Proteins Second messenger system biology.protein Intercellular Signaling Peptides and Proteins Peptides Protein Binding |
| Popis: | Phosphatidic acid is a phospholipid second messenger implicated in various cellular processes in eukaryotes. In plants, production of phosphatidic acid is triggered in response to a number of biotic and abiotic stresses. Here, we show that phosphatidic acid binds to 14-3-3 proteins, a family of regulatory proteins which bind client proteins in a phosphorylation-dependent manner. Binding of phosphatidic acid involves the same 14-3-3 region engaged in protein target binding. Consequently, micromolar phosphatidic acid concentrations significantly hamper the interaction of 14-3-3 proteins with the plasma membrane H(+)-ATPase, a well characterized plant 14-3-3 target, thus inhibiting the phosphohydrolitic enzyme activity. Moreover, the proton pump is inhibited when endogenous PA production is triggered by phospholipase D and the G protein agonist mastoparan-7. Hence, our data propose a possible mechanism involving PA that regulates 14-3-3-mediated cellular processes in response to stress. |
| Databáze: | OpenAIRE |
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