The 14-3-3 proteins: cellular regulators of plant metabolism

Chung, Hwa-Jee; Sehnke, Paul C.; Ferl, Robert J.

doi:10.1016/s1360-1385(99)01462-4

Cited by 142 publications

(85 citation statements)

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“…For several key enzymes, regulation of activity is a two-step process involving phosphorylation of the enzyme, followed by formation of a complex with 14-3-3 proteins to complete the regulatory transition (9,10). For example, the assimilation of nitrogen for production of amino acids or nucleotide bases is tightly controlled by nitrate reductase (NR).…”

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confidence: 99%

“…NR responds to environmental signals, such as light and metabolite levels, by phosphorylation and interacts with 14-3-3 proteins (11,12), thereby rapidly altering nitrogen flux according to the plant's metabolic requirements. This phosphorylation-dependent interaction of NR with 14-3-3 proteins has become a paradigm for posttranslational regulation of metabolic enzymes (9). Recently, 14-3-3 proteins have been identified inside plastids (13), thereby implicating a potential role in starch regulation.…”

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confidence: 99%

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Regulation of starch accumulation by granule-associated plant 14-3-3 proteins

Sehnke¹

2001

Proceedings of the National Academy of Sciences

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In higher plants the production of starch is orchestrated by chloroplast-localized biosynthetic enzymes, namely starch synthases, ADPglucose pyrophosphorylase, and starch branching and debranching enzymes. Diurnal regulation of these enzymes, as well as starchdegrading enzymes, influences both the levels and composition of starch, and is dependent in some instances upon phosphorylationlinked regulation. The phosphoserine͞threonine-binding 14-3-3 proteins participate in environmentally responsive phosphorylation-related regulatory functions in plants, and as such are potentially involved in starch regulation. We report here that reduction of the subgroup of Arabidopsis 14-3-3 proteins by antisense technology resulted in a 2-to 4-fold increase in leaf starch accumulation. Darkgoverned starch breakdown was unaffected in these "antisense plants," indicating an unaltered starch-degradation pathway and suggesting a role for 14-3-3 proteins in regulation of starch synthesis. Absorption spectra and gelatinization properties indicate that the starch from the antisense plants has an altered branched glucan composition. Biochemical characterization of protease-treated starch granules from both Arabidopsis leaves and maize endosperm showed that 14-3-3 proteins are internal intrinsic granule proteins. These data suggest a direct role for 14-3-3 proteins in starch accumulation. The starch synthase III family is a possible target for 14-3-3 protein regulation because, uniquely among plastid-localized starch metabolic enzymes, all members of the family contain the conserved 14-3-3 protein phosphoserine͞threonine-binding consensus motif. This possibility is strengthened by immunocapture using antibodies to DU1, a maize starch synthase III family member, and direct interaction with biotinylated 14-3-3 protein, both of which demonstrated an association between 14-3-3 proteins and DU1 or DU1-like proteins.

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Regulation of starch accumulation by granule-associated plant 14-3-3 proteins

Sehnke¹

2001

Proceedings of the National Academy of Sciences

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“…Members of the eukaryotic 14-3-3 family are highly conserved hydrophilic proteins that have been implicated in the regulation of diverse physiological processes by proteinprotein interactions (reviewed in Refs. [11][12][13]. Binding of 14-3-3 homologs to their target proteins appears to occur in a sequence-specific and phosphorylation-dependent manner (binding motif RSXpSXP (Ref.…”

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confidence: 99%

Binding of Regulatory 14-3-3 Proteins to the C Terminus of the Plant Plasma Membrane H+-ATPase Involves Part of Its Autoinhibitory Region

Jelich-Ottmann

Weiler

Oecking

2001

Journal of Biological Chemistry

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The plant plasma membrane H؉ -ATPase is activated by the binding of 14-3-3 proteins to its extreme C-terminal amino acids (YTV) and phosphorylation of the penultimate threonine (YpTV) is necessary for this interaction in vivo. However, in the presence of the fungal toxin fusicoccin (FC), binding of 14-3-3 proteins occurs independently of phosphorylation but still involves the YTV motif. Since FC exclusively binds to the complex consisting of both 14-3-3 homologs and the C-terminal domain of the H ؉ -ATPase, the toxin was used as a tool to reveal potential protein-protein interaction sites in the enzyme's C terminus. We performed in vitro interaction studies by applying various C-terminal parts of the H ؉ -ATPase PMA2 from Nicotiana plumbaginifolia expressed as glutathione S-transferase fusion peptides in E. coli. Interestingly, the PMA2 region encompassing residues 905-922 is implicated in FC-dependent binding of 14-3-3 homologs. Recently, part of this region has been shown to contribute to the autoinhibitory action of the PMA2 C terminus. Site-directed mutagenesis of individual amino acids localized within this region resulted in a drastic decrease in FC-dependent binding of 14-3-3 proteins. Furthermore, by expressing the corresponding mutants of PMA2 in yeast, we observed a reduced capability of the mutant enzymes to functionally replace the endogenous H ؉ -ATPase. Notably, the decreased activity of the mutant enzymes was accompanied by a weakened binding of yeast 14-3-3 homologs to the plasma membrane of transformed cells. Taken together, our results suggest that a section of the autoinhibitory C-terminal PMA2 region contributes to binding of activatory 14-3-3 proteins in the absence of FC.

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“…Both the N-terminus and the C-terminus of 14-3-3s are the crucial structures for the protein function. The N-terminus is related to the combination of the 14-3-3 protein with various membranes, while the C-terminus is directly involved in protein-protein interaction (Chung et al 1999).…”

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confidence: 99%

Molecular characterization of pear 14-3-3b gene regulated during fruit development

Shi

Zhao

et al. 2016

Can. J. Plant Sci.

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Plant 14-3-3 proteins (14-3-3s) are known to function in protein-protein interactions that mediate signal transduction pathways regulating many biological processes. The cDNA encoding putative 14-3-3 protein was isolated from pear (Pyrus pyrifolia) and designated Pp14-3-3b. Using the PCR amplification technique, the genomic clone corresponding to Pp14-3-3b was isolated and shown to contain six introns. Phylogenetic analysis clearly demonstrated that Pp14-3-3b was classified into the non-ε class of 14-3-3 superfamilies. Quantitative RT-PCR analysis indicated that the expression of the Pp14-3-3b gene was developmentally regulated in fruit. This study suggested that Pp14-3-3b might be involved in fruit ripening and the senescence of pear.Key words: pear (Pyrus pyrifolia), 14-3-3, gene expression, fruit development.Résumé : On sait que les protéines végétales 14-3-3 (14-3-3s) jouent un rôle dans les interactions entre protéines qui interviennent dans les voies de transduction des signaux régulant de nombreux processus biologiques. L'ADNc qui code la possible protéine 14-3-3 a été isolé chez le poirier (Pyrus pyrifolia) et désigné Pp14-3-3b. Par la technique d'amplification à la PCR, les auteurs ont isolé le clone génomique qui correspond à Pp14-3-3b et montré qu'il comporte six introns. L'analyse phylogénétique illustre clairement que Pp14-3-3b fait partie de la classe non-ε de la superfamille des 14-3-3. L'analyse par RT-PCR quantitative indique que l'expression du gène Pp14-3-3b est régulée par le développement chez le fruit. Cette étude laisse croire que le gène Pp14-3-3b pourrait contribuer au mûrissement du fruit et à la sénescence de la poire. [Traduit par la Rédaction]

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The 14-3-3 proteins: cellular regulators of plant metabolism

Cited by 142 publications

References 45 publications

Regulation of starch accumulation by granule-associated plant 14-3-3 proteins

Regulation of starch accumulation by granule-associated plant 14-3-3 proteins

Binding of Regulatory 14-3-3 Proteins to the C Terminus of the Plant Plasma Membrane H+-ATPase Involves Part of Its Autoinhibitory Region

Molecular characterization of pear 14-3-3b gene regulated during fruit development

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