A Protein Phosphatase 2C Involved in ABA Signal Transduction in
            <i>Arabidopsis thaliana</i>

Meyer, Knut; Leube, Martin P.; Grill, Erwin

doi:10.1126/science.8197457

Cited by 712 publications

(600 citation statements)

References 35 publications

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“…Subsequently 2-DE, in conjunction with immunoblotting, revealed that the heterogeneity of cruciferin isoforms far exceeded that predicted from the limited number of expressed genes and mRNA variants described above (Figure 3). The PP2C encoded by ABI1 has been implicated in the regulation of kinase signalling during seed development [29,30], and the abi1-1 mutant is known to exhibit pleiotropic effects. However, specific ABI1 targets have not yet been identified [33].…”

Section: Resultsmentioning

confidence: 99%

“…The ABI1 locus encodes a unique type of protein phosphatase in that the C-terminal domain possesses serine/ threonine protein phosphatase activity similar to that of PP2Cs (class 2C phosphatases), whereas the N-terminal domain contains a calcium-binding EF-hand motif that generally occurs only in the heterodimeric PP2B-type serine/threonine phosphatases. A single point mutation in the abi1-1 mutant significantly reduces PP2C activity [29,30], and genome-wide gene expression profiling indicates that ABA gene regulation is impaired [45]. Although recombinant fusion proteins containing either the whole ABI1 protein or only the phosphatase domain display in vitro phosphatase activity towards 32 P-labelled casein [46,47]; the in vivo targets have not yet been identified.…”

Section: Is Cruciferin An In Vivo Target For the Abi1 Protein Phosphamentioning

confidence: 99%

“…In the process, we discovered that the most abundant phosphorylated seed protein was cruciferin, and that multiple phosphorylation sites could be identified using LC-MS/MS (liquid chromatography-tandem MS). Since PP2C (protein phosphatase 2C), which is encoded by ABI1, has been implicated in the regulation of ABA (abscisic acid)-dependent kinase signalling during seed development [29,30], we also examined protein phosphorylation in the abi1-1 mutant, in which PP2C activity is significantly reduced. We found that cruciferin is hyperphosphorylated in this mutant and is, therefore, a probable target for the ABI1 protein phosphatase.…”

Section: Introductionmentioning

confidence: 99%

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Phosphorylation of the 12 S globulin cruciferin in wild-type and abi1-1 mutant Arabidopsis thaliana (thale cress) seeds

Wan

Ross

Yang

et al. 2007

Biochemical Journal

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Cruciferin (a 12 S globulin) is the most abundant storage protein in the seeds of Arabidopsis thaliana (thale cress) and other crucifers, sharing structural similarity with the cupin superfamily of proteins. Cruciferin is synthesized as a precursor in the rough endoplasmic reticulum. Subunit assembly is accompanied by structural rearrangements involving proteolysis and disulfidebond formation prior to deposition in protein storage vacuoles. The A. thaliana cv. Columbia genome contains four cruciferin loci, two of which, on the basis of cDNA analysis, give rise to three alternatively spliced variants. Using MS, we confirmed the presence of four variants encoded by genes At4g28520.1, At5g44120.3, At1g03880.1 and At1g3890.1 in A. thaliana seeds. Two-dimensional gel electrophoresis, along with immunological detection using anti-cruciferin antiserum and antibodies against phosphorylated amino acid residues, revealed that cruciferin was the major phosphorylated protein in Arabidopsis seeds and that polymorphism far exceeded that predicted on the basis of known isoforms. The latter may be attributed, at least in part, to phosphorylation site heterogeneity. A total of 20 phosphorylation sites, comprising nine serine, eight threonine and three tyrosine residues, were identified by MS. Most of these are located on the IE (interchain disulfide-containing) face of the globulin trimer, which is involved in hexamer formation. The implications of these findings for cruciferin processing, assembly and mobilization are discussed. In addition, the protein phosphatase 2C-impaired mutant, abi1-1, was found to exhibit increased levels of cruciferin phosphorylation, suggesting either that cruciferin may be an in vivo target for this enzyme or that abi1-1 regulates the protein kinase/phosphatase system required for cruciferin phosphorylation.

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Section: Resultsmentioning

confidence: 99%

Section: Is Cruciferin An In Vivo Target For the Abi1 Protein Phosphamentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Phosphorylation of the 12 S globulin cruciferin in wild-type and abi1-1 mutant Arabidopsis thaliana (thale cress) seeds

Wan

Ross

Yang

et al. 2007

Biochemical Journal

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“…These mutations were isolated 25-years ago by genetic screenings in Arabidopsis, aimed to the identification of ABAinsensitive mutants [27] and the cloning of the mutant loci provided pioneering insights into ABA signaling [28,29,30,31]. Both abi1-1D and abi2-1D are strong ABA-insensitive mutants that show diminished response to ABA in seeds and vegetative tissues, however, analysis of lossof-function alleles indicates that ABI1 and ABI2 gene products, as well as other clade A PP2Cs, are negative regulators of ABA signaling [32,33,34,35].…”

Section: Abi1-1 G180d Abi2-1 G168d and Hab1 G246d Hypermorphic Enzymesmentioning

confidence: 99%

Structural insights into PYR/PYL/RCAR ABA receptors and PP2Cs

et al. 2012

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Abscisic acid (ABA) plays an essential function in plant physiology since it is required for biotic and abiotic stress responses as well as control of plant growth and development. A new family of soluble ABA receptors, named PYR/PYL/RCAR, has emerged as ABA sensors able to inhibit the activity of specific protein phosphatases type-2C (PP2Cs) in an ABAdependent manner. The structural and functional mechanism by which ABA is perceived by these receptors and consequently leads to inhibition of the PP2Cs has been recently elucidated. The module PYR/PYL/RCAR-ABA-PP2C offers an elegant and unprecedented mechanism to control phosphorylation signaling cascades in a ligand-dependent manner. The knowledge of their three-dimensional structures paves the way to the design of ABA agonists able to modulate the plant stress response.

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“…The PP2C motifs described by Bork et al (1996) are surrounded by gray boxes. Black circles mark the locations of the lesions associated with two temperature-sensitive alleles of Ce-fem-2, b245, and q117 (Pilgrim et al 1995), and functionally mutant forms of the Arabidopsis PP2Cs ABI1 and ABI2 (Leung et al 1994(Leung et al , 1997Meyer et al 1994). The black asterisk marks the residue thought to bind phosphate ions, and the black diamonds indicate residues thought to bind metal ions (Das et al 1996).…”

Section: ) (F W Y) (K R H) (D E) (G a S) (P) (C) (T Nmentioning

confidence: 99%

Evolution of the PP2C Family in Caenorhabditis: Rapid Divergence of the Sex-Determining Protein FEM-2

Stothard

Hansen²,

Pilgrim³

2002

J Mol Evol

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Abstract. To investigate the causes and functional significance of rapid sex-determining protein evolution we compared three Caenorhabditis elegans genes encoding members of the protein phosphatase 2C (PP2C) family with their orthologs from another Caenorhabditis species (strain CB5161). One of the genes encodes FEM-2, a sex-determining protein, while the others have no known sex-determining role. FEM-2's PP2C domain was found to be more diverged than the other PP2C domains, supporting the notion that sex-determining proteins are subjected to selective pressures that allow for or cause rapid divergence. Comparison of the positions of amino acid substitutions in FEM-2 with a solved three-dimensional structure suggests that the catalytic face of the protein is highly conserved among C. elegans, CB5161, and another closely related species C. briggsae. However, the non-conserved regions of FEM-2 cannot be said to lack functional importance, since fem-2 transgenes from the other species were unable to rescue the germ-line defect caused by a C. elegans fem-2 mutation. To test whether fem-2 functions as a sex-determining gene in the other Caenorhabditis species we used RNA-mediated interference (RNAi). fem-2 (RNAi) in C. elegans and C. briggsae caused germ-line feminization, but had no noticeable effect in CB5161. Thus the function of fem-2 in CB5161 remains uncertain.

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A Protein Phosphatase 2C Involved in ABA Signal Transduction in Arabidopsis thaliana

Cited by 712 publications

References 35 publications

Phosphorylation of the 12 S globulin cruciferin in wild-type and abi1-1 mutant Arabidopsis thaliana (thale cress) seeds

Phosphorylation of the 12 S globulin cruciferin in wild-type and abi1-1 mutant Arabidopsis thaliana (thale cress) seeds

Structural insights into PYR/PYL/RCAR ABA receptors and PP2Cs

Evolution of the PP2C Family in Caenorhabditis: Rapid Divergence of the Sex-Determining Protein FEM-2

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