Journal
PHYSIOLOGIA PLANTARUM
Volume 128, Issue 2, Pages 334-340Publisher
WILEY
DOI: 10.1111/j.1399-3054.2006.00757.x
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The activity of the plant plasma membrane H+-ATPase is tightly regulated via phosphorylation and binding of 14-3-3 protein to the C-terminus of the pump. Whereas the 14-3-3-binding mechanism has been described in detail, the identity of specific protein kinases and phosphatases involved in the control of 14-3-3 binding has remained elusive. Using the yeast two-hybrid system, GST pull-down assays and overlay experiments, we report that scaffolding subunit A of protein phosphatase 2A (PP2A-A) interacts with the C-terminus of the Arabidopsis plasma membrane H+-ATPase isoform 2. PP2A-A binding is inhibited in the presence of 14-3-3 protein and fusicoccin, a fungal toxin which induces binding of 14-3-3 protein to the C-terminal end of the plasma membrane H+-ATPase. This indicates that PP2A-A and 14-3-3 protein compete with each other for binding to the same region in the C-terminus of the H+-ATPase.
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