The Arabidopsis 14-3-3 Family of Signaling Regulators

DeLille, Justin M.; Sehnke, Paul C.; Ferl, Robert J.

doi:10.1104/pp.126.1.35

Cited by 169 publications

(164 citation statements)

References 16 publications

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“…Based on exon numbers, 14-3-3 proteins are divided into an ⑀ group (6 -7 exons, five members) and a plant-specific non-⑀ group (four exons, seven members in three subgroups) (15). Thus Arabidopsis 14-3-3 proteins form a functionally heterogeneous group (with four subgroups) on the basis of both their diverse gene and expression pattern as well as cellular localization (16,17).…”

Section: -3-3 Proteins Regulate Key Processes In Eukaryotic Cellsmentioning

confidence: 99%

Molecular Mechanism of 14-3-3 Protein-mediated Inhibition of Plant Nitrate Reductase

Lambeck

Fischer-Schrader

Niks

et al. 2012

Journal of Biological Chemistry

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Background: Plant nitrate reductase activity is regulated by phosphorylation and subsequent 14-3-3 protein binding. Results: Steady-state and pre-steady kinetics revealed the electron transfer rates between all three redox-active cofactors and identified the heme-to-molybdenum transfer as key regulatory point. Conclusion: 14-3-3 proteins inhibit domain movement in nitrate reductase. Significance: This is the first description of 14-3-3-regulated electron transfer in a multidomain metallo-enzyme.

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Section: -3-3 Proteins Regulate Key Processes In Eukaryotic Cellsmentioning

confidence: 99%

Molecular Mechanism of 14-3-3 Protein-mediated Inhibition of Plant Nitrate Reductase

Lambeck

Fischer-Schrader

Niks

et al. 2012

Journal of Biological Chemistry

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“…Arabidopsis, 14-3-3 proteins consist of 13 isoforms, and each isoform can be separated into two major evolutionary branches, the ⑀ group and the non-⑀ group (39). Each isoform has a different binding affinity to the client proteins (40,41).…”

Section: The 14-3-3 Proteins Interact With the C-terminal Region Of Amentioning

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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“…In Arabidopsis, there are up to 15 members of the 14-3-3 family [73]. They are categorized by sequence into groups and isoforms.…”

Section: Discussionmentioning

confidence: 99%

Identification of a host 14-3-3 protein that interacts with Xanthomonas effector AvrRxv

Whalen

Richter

Zakhareyvich

et al. 2008

Physiological and Molecular Plant Pathology

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AvrRxv is a member of a family of pathogen effectors present in pathogens of both plant and mammalian species. Xanthomonas campestris pv. vesicatoria strains carrying AvrRxv induce a hypersensitive response (HR) in the tomato cultivar Hawaii 7998. Using a yeast two-hybrid screen, we identified a 14-3-3 protein from tomato that interacts with AvrRxv called AvrRxv Interactor 1 (ARI1). The interaction was confirmed in vitro with affinity chromatography. Using mutagenesis, we identified a 14-3-3-binding domain in AvrRxv and demonstrated that a mutant in that domain showed concomitant loss of interaction with ARI1 and HR-inducing activity in tomato. These results demonstrate that the AvrRxv bacterial effector recruits 14-3-3 proteins for its function within host cells. AvrRxv homologues YopP and YopJ from Yersinia do not have AvrRxv-specific HR-inducing activity when delivered into tomato host cells by Agrobacterium. Although YopP itself cannot induce HR, its C-terminal domain containing the catalytic residues can replace that of AvrRxv in an AvrRxv-YopP chimera for HR-inducing activity. Phylogenetic analysis indicates that the sequences encoding the C-termini of family members are evolving independently from those encoding the N-termini. Our results support a model in which there are three functional domains in proteins of the family, translocation, interaction, and catalytic.

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The Arabidopsis 14-3-3 Family of Signaling Regulators

Cited by 169 publications

References 16 publications

Molecular Mechanism of 14-3-3 Protein-mediated Inhibition of Plant Nitrate Reductase

Molecular Mechanism of 14-3-3 Protein-mediated Inhibition of Plant Nitrate Reductase

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

Identification of a host 14-3-3 protein that interacts with Xanthomonas effector AvrRxv

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