Phosphorylation of Thr-948 at the C Terminus of the Plasma Membrane H+-ATPase Creates a Binding Site for the Regulatory 14-3-3 Protein

Phosphorylation of Thr-948 at the C Terminus of the Plasma Membrane H+-ATPase Creates a Binding Site for the Regulatory 14-3-3 Protein. Svennelid, F., Olsson, A., Piotrowski, M., Rosenquist, M., Ottman, C., Larsson, C., Oecking, C., & Sommarin, M. The Plant Cell, 11(12):2379–2391, December, 1999.

Paper doi abstract bibtex

The plant plasma membrane H+-ATPase is activated by the binding of 14-3-3 protein to the C-terminal region of the enzyme, thus forming an H+-ATPase–14-3-3 complex that can be stabilized by the fungal toxin fusicoccin. A novel 14-3-3 binding motif, QQXYpT948V, at the C terminus of the H+-ATPase is identified and characterized, and the protein kinase activity in the plasma membrane fraction that phosphorylates this threonine residue in the H+-ATPase is identified. A synthetic peptide that corresponds to the C-terminal 16 amino acids of the H+-ATPase and that is phosphorylated on Thr-948 prevents the in vitro activation of the H+-ATPase that is obtained in the presence of recombinant 14-3-3 and fusicoccin. Furthermore, binding of 14-3-3 to the H+-ATPase in the absence of fusicoccin is absolutely dependent on the phosphorylation of Thr-948, whereas binding of 14-3-3 in the presence of fusicoccin occurs independently of phosphorylation but still involves the C-terminal motif YTV. Finally, by complementing yeast that lacks its endogenous H+-ATPase with wild-type and mutant forms of the Nicotiana plumbaginifolia H+-ATPase isoform PMA2, we provide physiological evidence for the importance of the phosphothreonine motif in 14-3-3 binding and, hence, in the activation of the H+-ATPase in vivo. Indeed, replacing Thr-948 in the plant H+-ATPase with alanine is lethal because this mutant fails to functionally replace the yeast H+-ATPase. Considering the importance of the motif QQXYpTV for 14-3-3 binding and yeast growth, this motif should be of vital importance for regulating H+-ATPase activity in the plant and thus for plant growth.

@article{svennelid_phosphorylation_1999,
	title = {Phosphorylation of {Thr}-948 at the {C} {Terminus} of the {Plasma} {Membrane} {H}+-{ATPase} {Creates} a {Binding} {Site} for the {Regulatory} 14-3-3 {Protein}},
	volume = {11},
	issn = {1040-4651},
	url = {https://doi.org/10.1105/tpc.11.12.2379},
	doi = {10/d8hvv3},
	abstract = {The plant plasma membrane H+-ATPase is activated by the binding of 14-3-3 protein to the C-terminal region of the enzyme, thus forming an H+-ATPase–14-3-3 complex that can be stabilized by the fungal toxin fusicoccin. A novel 14-3-3 binding motif, QQXYpT948V, at the C terminus of the H+-ATPase is identified and characterized, and the protein kinase activity in the plasma membrane fraction that phosphorylates this threonine residue in the H+-ATPase is identified. A synthetic peptide that corresponds to the C-terminal 16 amino acids of the H+-ATPase and that is phosphorylated on Thr-948 prevents the in vitro activation of the H+-ATPase that is obtained in the presence of recombinant 14-3-3 and fusicoccin. Furthermore, binding of 14-3-3 to the H+-ATPase in the absence of fusicoccin is absolutely dependent on the phosphorylation of Thr-948, whereas binding of 14-3-3 in the presence of fusicoccin occurs independently of phosphorylation but still involves the C-terminal motif YTV. Finally, by complementing yeast that lacks its endogenous H+-ATPase with wild-type and mutant forms of the Nicotiana plumbaginifolia H+-ATPase isoform PMA2, we provide physiological evidence for the importance of the phosphothreonine motif in 14-3-3 binding and, hence, in the activation of the H+-ATPase in vivo. Indeed, replacing Thr-948 in the plant H+-ATPase with alanine is lethal because this mutant fails to functionally replace the yeast H+-ATPase. Considering the importance of the motif QQXYpTV for 14-3-3 binding and yeast growth, this motif should be of vital importance for regulating H+-ATPase activity in the plant and thus for plant growth.},
	number = {12},
	urldate = {2021-11-08},
	journal = {The Plant Cell},
	author = {Svennelid, Fredrik and Olsson, Anne and Piotrowski, Markus and Rosenquist, Magnus and Ottman, Cristian and Larsson, Christer and Oecking, Claudia and Sommarin, Marianne},
	month = dec,
	year = {1999},
	pages = {2379--2391},
}

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A novel 14-3-3 binding motif, QQXYpT948V, at the C terminus of the H+-ATPase is identified and characterized, and the protein kinase activity in the plasma membrane fraction that phosphorylates this threonine residue in the H+-ATPase is identified. A synthetic peptide that corresponds to the C-terminal 16 amino acids of the H+-ATPase and that is phosphorylated on Thr-948 prevents the in vitro activation of the H+-ATPase that is obtained in the presence of recombinant 14-3-3 and fusicoccin. Furthermore, binding of 14-3-3 to the H+-ATPase in the absence of fusicoccin is absolutely dependent on the phosphorylation of Thr-948, whereas binding of 14-3-3 in the presence of fusicoccin occurs independently of phosphorylation but still involves the C-terminal motif YTV. 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