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Arabidopsis NRP switches off the PP6 phosphatase FyPP3 to repress auxin-mediated growth in response to abscisic acid

ABSTRACT: Arabidopsis NRP switches off the PP6 phosphatase FyPP3 to repress auxin-mediated growth in response to abscisic acid

PROVIDER: PRJNA633096 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR11795800_1.fastq.gz	Fastqsanger.gz
	SRR11795800_2.fastq.gz	Fastqsanger.gz
	SRR11795801_1.fastq.gz	Fastqsanger.gz
	SRR11795801_2.fastq.gz	Fastqsanger.gz
	SRR11795802_1.fastq.gz	Fastqsanger.gz

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Arabidopsis NRP switches off the PP6 phosphatase FyPP3 to repress auxin-mediated growth in response to abscisic acid

Project description:How environmentally challenged plants can switch from growth to stress adaptation is an important question in plant physiology. To identify the key regulatory proteins and to characterize the underlying signaling pathways are essential in answering this question. Here we show that the abiotic stress hormone Abscisic acid (ABA) induces the expression of the Asparagine rich proteins (NRP), DCD1 and DCD2, to repress the auxin-induced growth by promoting vacuolar degradation of PIN2, the auxin efflux carrier. ABA-induced degradation of PIN2 is inhibited in the dcd1 dcd2 double mutant, and inhibition of FyPP3, the catalytic subunit of the PP6 protein phosphatase, can restore the PIN recycling and growth phenotype in the double mutant. Transcriptome analyses on WT, dcd1 dcd2, the FyPP3 Dominant Negative line (FyPP3-DN), and dcd1 dcd2/FyPP3-DN supported the essential function of the NRP-FyPP3 module in the growth- to stress-response switch.

2020-05-16 | GSE150648 | GEO

Arabidopsis thaliana

Project description:Arabidopsis NRP switches off the PP6 phosphatase FyPP3 to repress auxin-mediated growth in response to abscisic acid

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Arabidopsis PP6 phosphatases dephosphorylate PIF proteins to repress photomorphogenesis.

Project description:Light-induced phosphorylation is necessary and essential for the degradation of phytochrome-interacting factors (PIFs), the central repressors of photomorphogenesis. Although the kinases responsible for PIF phosphorylation have been extensively studied, the phosphatases underlying PIF dephosphorylation are largely unknown. Here, we real that mutation of FyPP1 and FyPP3, two catalytic subunits of PP6 phosphatases, promoted photomorphogenesis of seedlings in the dark. PP6 and PIFs functioned synergistically to repress photomorphogenesis. FyPP1 and FyPP3 directly interacted with and dephosphorylated PIF3 and PIF4. The light-induced degradation of PIF4 and the PIF transcriptional activities were dependent on PP6 activity. These data demonstrate that PP6 phosphatases repress photomorphogenesis through regulation of PIF phosphorylation, protein stability and transcriptional activity.

2019-09-04 | GSE128498 | GEO

Arabidopsis PP6 phosphatases dephosphorylate PIF proteins to repress photomorphogenesis.

Project description:Arabidopsis PP6 phosphatases dephosphorylate PIF proteins to repress photomorphogenesis.

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Adaptation of HepG2 Cells to a Steady-State Reduction in the Content of Protein Phosphatase 6 (PP6) Catalytic Subunit

Project description:To assess the potential of PP6 as a therapeutic target in liver disorders, we attenuated expression of the PP6 catalytic subunit in HepG2 cells using lentiviral-transduced shRNA. Two PP6 knock-down (PP6KD) cell lines 18.5 and 19.5, (90% reduction of PP6-C protein content) were studied in depth. Both proliferated at a rate similar to control cells. However, flow cytometry indicated G2/M cell cycle arrest that was accounted for by a shift of the cells from a diploid to tetraploid state. PP6KD cells did not show an increase in apoptosis, nor did they exhibit reduced viability in the presence of bleomycin. Gene expression analysis by microarray showed attenuated anti-inflammatory signaling. Genes associated with DNA replication were downregulated. Mass spectrometry-based phosphoproteomic analysis yielded 80 phosphopeptides representing 56 proteins that were significantly affected by a stable reduction in PP6-C. Proteins involved in DNA replication, DNA damage repair and pre-mRNA splicing were overrepresented among these. PP6KD cells showed intact mTOR signaling.

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Widespread N6-methyladenosine-dependent RNA Structural Switches Regulate RNA-Protein Interactions

Project description:We show that N6-methyladenosine (m6A), the most abundant internal modification in mRNA/lncRNA with still poorly characterized function, alters RNA structure to facilitate the access of RBM for heterogeneous nuclear ribonucleoprotein C (hnRNP C). We term this mechanism m6A-switch. Through combining PAR-CLIP with Me-RIP, we identify 39,060 m6A-switches among hnRNP C binding sites transcriptome-wide. We show that m6A-methyltransferases METTL3 or METTL14 knockdown decreases hnRNP C binding at 16,582 m6A-switches. Taken together, 2,798 m6A-switches of high confidence are identified to mediate RNA-hnRNP C interactions and affect diverse biological processes including cell cycle regulation. These findings reveal the biological importance of m6A and provide insights into the sophisticated regulation of RNA-RBP interactions through m6A-induced RNA structural remodeling.

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