14-3-3 proteins in plant physiology

Denison, Fiona C.; Paul, Anna‐Lisa; Zupanska, Agata K.; Ferl, Robert J.

doi:10.1016/j.semcdb.2011.08.006

Cited by 241 publications

(183 citation statements)

References 118 publications

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“…In seeds, the 14-3-3 (Table 2) appears to be ABAdependent protein (Testerink et al 1999) involved in the stress signal transduction pathway because this protein is phosphorylated by SnRK.8, an important kinase for drought resistance (Denison et al 2011). Via interactions with phosphorylated proteins 14-3-3 modulates their function and consequently regulates transport through ion channels, virulence-mediated programmed cell death, ROS production as a defense mechanism and microtubule cell arrangement (Denison et al 2011).…”

Section: Identification Of Carbonylated Proteinsmentioning

confidence: 99%

“…Via interactions with phosphorylated proteins 14-3-3 modulates their function and consequently regulates transport through ion channels, virulence-mediated programmed cell death, ROS production as a defense mechanism and microtubule cell arrangement (Denison et al 2011). Therefore, in long-term stored seeds, many biochemical traits might be modified, thus contributing to the no-germination seed phenotype.…”

Section: Identification Of Carbonylated Proteinsmentioning

confidence: 99%

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Carbonylated proteins accumulated as vitality decreases during long-term storage of beech (Fagus sylvatica L.) seeds

Kalemba

Pukacka

2013

Trees

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Key message Carbonylation of proteins associated with a stress response may contribute to the lowered viability of naturally aged beech seeds, especially the desiccation tolerance-associated proteins and USP-like protein.Abstract Proteins are modified by a large number of reactions that involve reactive oxygen species-mediated oxidation. The direct oxidation of amino acids produces 2,4-dinitrophenylhydrazine-detectable protein products. Carbonylation is irreversible, and carbonylated proteins are marked for proteolysis or can escape degradation and form high molecular weight aggregates, which accumulate with age. Beech (Fagus sylvatica L.) seeds stored under optimal conditions for different periods of time, ranging from 2 to 13 years, were analyzed. Protein carbonylation was examined as a potential cause for the loss of viability of beech seeds, and the characteristic spots of protein carbonyls were identified. Here, we present and discuss the role of carbonylation in the proteome of beech seeds that contribute to the loss of seed viability during natural aging. The long-term storage of beech seeds is intricate because their germination capacity decreases with age and is negatively correlated with the level of protein carbonyls that accumulate in the seeds. We establish that protein synthesis, folding and degradation are the most affected biochemical traits in long-term stored beech seeds. In addition, we suggest that proteins associated with the stress response may have contributed to the lowered viability of beech seeds, especially the desiccation toleranceassociated proteins that include T-complex protein 1 and the universal stress protein (USP)-like protein, which is identified as carbonylated for first time here.

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Section: Identification Of Carbonylated Proteinsmentioning

confidence: 99%

Section: Identification Of Carbonylated Proteinsmentioning

confidence: 99%

Carbonylated proteins accumulated as vitality decreases during long-term storage of beech (Fagus sylvatica L.) seeds

Kalemba

Pukacka

2013

Trees

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“…14-3-3 proteins are a family of evolutionary conserved dimeric proteins that accomplish a wide range of regulatory roles in eukaryotes (Fu et al, 2000). In plants, in addition to the plasma membrane transport through the regulation of the H þ -ATPase activity, 14-3-3s are involved in the control of gene expression, in the cellular trafficking, in the control of the activities of diverse enzymes of metabolism, in the hormone signaling, and in general in the coordination of different signal transduction pathways (Aducci et al, 2002;Sottocornola et al, 2006;Camoni et al, 2011;Schoonheim et al, 2009;Denison et al, 2011). Lots of evidence suggest also a role of 14-3-3s in the plant response to stress conditions (G€ okirmak et al, 2010): environmental and biotic stresses can affect the expression levels of 14-3-3 genes (Chevalier et al, 2009) and also a large number of stresserelated proteins have been identified as 14-3-3 clients (Chang et al, 2009).…”

Section: Introductionmentioning

confidence: 99%

Cold stress affects H + -ATPase and phospholipase D activity in Arabidopsis

Muzi

Camoni

Visconti

et al. 2016

Plant Physiology and Biochemistry

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a b s t r a c tLow temperature is an environmental stress that greatly influences plant performance and distribution. Plants exposed to cold stress exhibit modifications of plasma membrane physical properties that can affect their functionality. Here it is reported the effect of low temperature exposure of Arabidopsis plants on the activity of phospholipase D and H þ -ATPase, the master enzyme located at the plasma membrane.The H þ -ATPase activity was differently affected, depending on the length of cold stress imposed. In particular, an exposure to 4 C for 6 h determined the strong inhibition of the H þ -ATPase activity, that correlates with a reduced association with the regulatory 14-3-3 proteins. A longer exposure first caused the full recovery of the enzymatic activity followed by a significant activation, in accordance with both the increased association with 14-3-3 proteins and induction of H þ -ATPase gene transcription. Different time lengths of cold stress treatment were also shown to strongly stimulate the phospholipase D activity and affect the phosphatidic acid levels of the plasma membranes. Our results suggest a functional correlation between the activity of phospholipase D and H þ -ATPase mediated by phosphatidic acid release during the cold stress response.

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“…Subsequent proteomic analyses identified 14-3-3 proteins as interactors of ATL31 (12). 14-3-3 proteins bind to phosphorylated motifs and function in multiple developmental processes by regulating the activity of a wide variety of target proteins (13)(14)(15). In particular, 14-3-3 proteins have been reported to regulate primary carbon and nitrogen metabolism by directly interacting with key enzymes (16 -18).…”

mentioning

confidence: 99%

Phosphorylation of Arabidopsis Ubiquitin Ligase ATL31 Is Critical for Plant Carbon/Nitrogen Nutrient Balance Response and Controls the Stability of 14-3-3 Proteins

Yasuda

Sato

Maekawa

et al. 2014

Journal of Biological Chemistry

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Background: Ubiquitin ligase ATL31 and the target, 14-3-3 proteins, function in plant nutrient response. Results: ATL31 binds to 14-3-3 proteins via phosphorylation of specific residues. These residues are essential for the function of ATL31. Conclusion: ATL31 targets 14-3-3 proteins for degradation in a phosphorylation-dependent manner to regulate nutrient response. Significance: Phosphorylation of ubiquitin ligase ATL31 controls plant nutrient response.

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14-3-3 proteins in plant physiology

Cited by 241 publications

References 118 publications

Carbonylated proteins accumulated as vitality decreases during long-term storage of beech (Fagus sylvatica L.) seeds

Carbonylated proteins accumulated as vitality decreases during long-term storage of beech (Fagus sylvatica L.) seeds

Cold stress affects H + -ATPase and phospholipase D activity in Arabidopsis

Phosphorylation of Arabidopsis Ubiquitin Ligase ATL31 Is Critical for Plant Carbon/Nitrogen Nutrient Balance Response and Controls the Stability of 14-3-3 Proteins

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