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Binding of phosphatidic acid to 14‐3‐3 proteins hampers their ability to activate the plant plasma membrane H + ‐ATPase
Author(s) -
Camoni Lorenzo,
Di Lucente Cristina,
Pallucca Roberta,
Visconti Sabina,
Aducci Patrizia
Publication year - 2012
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1002/iub.1058
Subject(s) - phosphatidic acid , mastoparan , biochemistry , phospholipase d , second messenger system , chemistry , microbiology and biotechnology , phospholipid , atpase , biology , membrane , enzyme , signal transduction , g protein
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. © 2012 IUBMB IUBMB Life, 64(8): 710–716, 2012