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.
Identifieur interne : 000098 ( Pmc/Curation ); précédent : 000097; suivant : 000099Phosphorylation of Thr-948 at the C terminus of the plasma membrane H(+)-ATPase creates a binding site for the regulatory 14-3-3 protein.
Auteurs : F. Svennelid ; A. Olsson ; M. Piotrowski ; M. Rosenquist ; C. Ottman ; C. Larsson ; C. Oecking ; M. SommarinSource :
- The Plant Cell [ 1040-4651 ] ; 1999.
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, QQXYpT(948)V, 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.
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PubMed: 10590165
PubMed Central: 144135
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<author><name sortKey="Piotrowski, M" sort="Piotrowski, M" uniqKey="Piotrowski M" first="M" last="Piotrowski">M. Piotrowski</name>
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<author><name sortKey="Rosenquist, M" sort="Rosenquist, M" uniqKey="Rosenquist M" first="M" last="Rosenquist">M. Rosenquist</name>
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<author><name sortKey="Ottman, C" sort="Ottman, C" uniqKey="Ottman C" first="C" last="Ottman">C. Ottman</name>
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<author><name sortKey="Larsson, C" sort="Larsson, C" uniqKey="Larsson C" first="C" last="Larsson">C. Larsson</name>
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<series><title level="j">The Plant Cell</title>
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<front><div type="abstract" xml:lang="en"><p>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, QQXYpT(948)V, 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.</p>
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<pmc article-type="research-article"><pmc-comment>The publisher of this article does not allow downloading of the full text in XML form.</pmc-comment>
<front><journal-meta><journal-id journal-id-type="nlm-ta">Plant Cell</journal-id>
<journal-title>The Plant Cell</journal-title>
<issn pub-type="ppub">1040-4651</issn>
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<article-categories><subj-group subj-group-type="heading"><subject>Research Article</subject>
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<title-group><article-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.</article-title>
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<contrib-group><contrib contrib-type="author"><name><surname>Svennelid</surname>
<given-names>F</given-names>
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<contrib contrib-type="author"><name><surname>Olsson</surname>
<given-names>A</given-names>
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<contrib contrib-type="author"><name><surname>Piotrowski</surname>
<given-names>M</given-names>
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<contrib contrib-type="author"><name><surname>Rosenquist</surname>
<given-names>M</given-names>
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<contrib contrib-type="author"><name><surname>Ottman</surname>
<given-names>C</given-names>
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<contrib contrib-type="author"><name><surname>Larsson</surname>
<given-names>C</given-names>
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<contrib contrib-type="author"><name><surname>Oecking</surname>
<given-names>C</given-names>
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<contrib contrib-type="author"><name><surname>Sommarin</surname>
<given-names>M</given-names>
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<aff>Department of Plant Biochemistry, Lund University, P.O. Box 117, SE-221 00 Lund, Sweden.</aff>
<pub-date pub-type="ppub"><month>12</month>
<year>1999</year>
</pub-date>
<volume>11</volume>
<issue>12</issue>
<fpage>2379</fpage>
<lpage>2391</lpage>
<abstract><p>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, QQXYpT(948)V, 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.</p>
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