Summary

Baunsgaard, Lone; Fuglsang, Anja Thoe; Jahn, Thomas P.; Korthout, Henrie A. A. J.; Boer, Albertus H. de; Palmgren, Michael G.

doi:10.1046/j.1365-313x.1998.00083.x

Cited by 199 publications

(60 citation statements)

References 49 publications

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“…FC-binding Properties of Mutated AHA2 Protein-The binding site for FC is complex, since this compound interacts with both 14-3-3 protein and the C-terminal region of plant plasma membrane H ϩ -ATPase (15,26). To investigate the role of Thr-924 and nearby residues in FC binding to nonphosphorylated H ϩ -ATPase, full-length AHA2 proteins carrying substitutions in the stretch from Glu-921 to Leu-925 were expressed in yeast, and membranes of yeast endoplasmic reticulum enriched in recombinant plant enzyme were isolated.…”

Section: Identification Of Single Residues Essential For Phosphorylatmentioning

confidence: 99%

“…Most secondary transporters in plant cells depend upon the activity of the plasma membrane H ϩ -ATPase, which is essential for generating the electrochemical gradient across the plasma membrane (for a review, see Ref. 14), and it has therefore generated considerable interest that 14-3-3 proteins have appeared as positive regulators of this proton pump (15).…”

mentioning

confidence: 99%

“…FC binding requires the simultaneous presence of 14-3-3 and the C-terminal end of H ϩ -ATPase (15,24,25). A plant 14-3-3 protein was recently co-crystallized with FC and a phosphorylated peptide (QSYpTV) representing the five C-terminal residues of a tobacco plasma membrane H ϩ -ATPase isoform (26).…”

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confidence: 99%

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The Binding Site for Regulatory 14-3-3 Protein in Plant Plasma Membrane H+-ATPase

Fuglsang¹,

Borch

Bych³

et al. 2003

Journal of Biological Chemistry

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. We report binding of 14-3-3 protein to a nonphosphorylated peptide representing the 34 C-terminal residues of the Arabidopsis plasma membrane H ؉ -ATPase isoform 2 (AHA2). Following site-directed mutagenesis within the 45 C-terminal residues of AHA2, we conclude that, in addition to the 946 YpTV motif, a number of residues located further upstream are required for phosphorylation-independent binding of 14-3-3. Among these, Thr-924 is important for interaction with 14-3-3 protein even when Thr-947 is phosphorylated. We suggest that the role of phosphorylation, which is accentuated by fusicoccin, is to stabilize protein-protein interaction between 14-3-3 protein and several residues of the H ؉ -ATPase C-terminal domain.

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Section: Identification Of Single Residues Essential For Phosphorylatmentioning

confidence: 99%

mentioning

confidence: 99%

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The Binding Site for Regulatory 14-3-3 Protein in Plant Plasma Membrane H+-ATPase

Fuglsang¹,

Borch

Bych³

et al. 2003

Journal of Biological Chemistry

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“…Also, the amount of FC bound to plasma membrane appears to be strictly correlated with stimulation of H ϩ -ATPase activity (12). More recent evidence indicates that administration of FC in vivo or in vitro stabilizes (13) or promotes (14) the interaction between H ϩ -ATPase and 14-3-3 proteins.…”

mentioning

confidence: 94%

Fusicoccin Effect on the in Vitro Interaction between Plant 14-3-3 Proteins and Plasma Membrane H+-ATPase

Fullone¹,

Visconti²,

Marra³

et al. 1998

Journal of Biological Chemistry

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A 17-amino acid peptide was selectively cleaved from the highly variant C terminus of the 33-kDa 14-3-3 isoform occurring in fusicoccin receptor preparations from maize and was sequenced. The determined C-terminal sequence was identical to that of the already known maize 14-3-3 homolog GF14-6, thus prompting the use of recombinant GF14-6 in an in vitro protein-protein interaction study. The cDNA of GF14-6 was expressed in Escherichia coli as a 32 P-phosphorylatable glutathione S-transferase fusion protein and was used as a probe in overlay experiments with H ؉ -ATPase partially purified from maize roots. The results demonstrated that the recombinant protein specifically bound to H ؉ -ATPase. The binding was dependent on Mg 2؉ and was strongly increased by fusicoccin. Controlled trypsin digestion of H ؉ -ATPase abolished the association with GF14-6, a finding that was suggestive of an interaction with the C terminus of the enzyme. To confirm this result, the Cterminal domain of H ؉ -ATPase was expressed as a glutathione S-transferase fusion peptide and was used in overlay experiments. GF14-6 was also able to bind to the isolated C terminus, but only in the presence of fusicoccin.

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“…In plants, consumers of energy and reducing power produced by the chloroplasts and mitochondria-e.g., the plasma membrane H ϩ ATPase (P type), nitrate reductase (NR), sucrosephosphate synthase (SPS), trehalose-6-phosphate synthase, and plasma membrane K ϩ channels-are all regulated by 14-3-3 proteins (17)(18)(19). A picture is emerging wherein 14-3-3 proteins play a central role in controlling the primary metabolism of plants, and the question arises whether activities are coordinately regulated by the different 14-3-3 isoforms present in plants.…”

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confidence: 99%

14-3-3 protein is a regulator of the mitochondrial and chloroplast ATP synthase

Bunney

Walraven

Boer

2001

Proc. Natl. Acad. Sci. U.S.A.

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Mitochondrial and chloroplast ATP synthases are key enzymes in plant metabolism, providing cells with ATP, the universal energy currency. ATP synthases use a transmembrane electrochemical proton gradient to drive synthesis of ATP. The enzyme complexes function as miniature rotary engines, ensuring energy coupling with very high efficiency. Although our understanding of the structure and functioning of the synthase has made enormous progress in recent years, our understanding of regulatory mechanisms is still rather preliminary. Here we report a role for 14-3-3 proteins in the regulation of ATP synthases. These 14-3-3 proteins are highly conserved phosphoserine͞phosphothreonine-binding proteins that regulate a wide range of enzymes in plants, animals, and yeast. Recently, the presence of 14-3-3 proteins in chloroplasts was illustrated, and we show here that plant mitochondria harbor 14-3-3s within the inner mitochondrial-membrane compartment. There, the 14-3-3 proteins were found to be associated with the ATP synthases, in a phosphorylation-dependent manner, through direct interaction with the F 1 ␤-subunit. The activity of the ATP synthases in both organelles is drastically reduced by recombinant 14-3-3. The rapid reduction in chloroplast ATPase activity during dark adaptation was prevented by a phosphopeptide containing the 14-3-3 interaction motif, demonstrating a role for endogenous 14-3-3 in the down-regulation of the CF oF1 activity. We conclude that regulation of the ATP synthases by 14-3-3 represents a mechanism for plant adaptation to environmental changes such as light͞dark transitions, anoxia in roots, and fluctuations in nutrient supply.

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Summary

Cited by 199 publications

References 49 publications

The Binding Site for Regulatory 14-3-3 Protein in Plant Plasma Membrane H+-ATPase

The Binding Site for Regulatory 14-3-3 Protein in Plant Plasma Membrane H+-ATPase

Fusicoccin Effect on the in Vitro Interaction between Plant 14-3-3 Proteins and Plasma Membrane H+-ATPase

14-3-3 protein is a regulator of the mitochondrial and chloroplast ATP synthase

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