Ontology highlight
ABSTRACT:
PROVIDER: PRJNA678744 | ENA |
REPOSITORIES: ENA
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| SRR13068611.fastq.gz | Fastqsanger.gz | |||
| SRR13068612.fastq.gz | Fastqsanger.gz | |||
| SRR13068613.fastq.gz | Fastqsanger.gz | |||
| SRR13068614.fastq.gz | Fastqsanger.gz | |||
| SRR13068615.fastq.gz | Fastqsanger.gz |
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Project description:MicroRNAs and phytophormes are all small molecular signals that play important roles in regulating development and environmental responses in plants. The interplay between them allow the plants to better converge multiple inner and outer signals to optimizing their survival strategy. So far, the knowledge of how miRNAs are involved in brassinosteroid (BR) signaling is lacking. Here, we report the finding of miR394 and its target gene LEAF CURLING RESPONSENESS (LCR), which were transcriptionally responsive to BR, participate in BR signaling in regulating hypocotyls elongation in Arabidopsis. By phenotypic analyzing of a set of transgenic and mutants, miR394 was found to act as a negative regulator in BR signaling in hypocotyls elongation, while its target gene on the contrary. Genetically, miR394 functions upstream of BIN2 and BZR1/BES1, but partially downstream or independent with BRI1 and BSU1. RNA-seq analysis further supports that miR394 inhibits BR signaling through BIN2 because miR394 co-regulate significant number of genes together with BIN2. Additionally, miR394 improved the accumulation of BIN2 but decreased the protein amount of BZR1 and BES1, which can be phosphorylated by BIN2. miR394 also repressed the transcription of PRE1/5/6 and EXP8, the key hypocotyls elongation regulating genes, which had been reported to be BZR1/BES1 targets. These findings revealed a new pathway that miRNA involved in BR signaling in Arabidopsis.
2019-08-01 | GSE114214 | GEO
Project description:Transient protein-protein interactions (PPIs), such as those between posttranslational modifying enzymes and their substrates, play key roles in cellular regulation, but are difficult to identify. Here we demonstrate the application of enzyme-catalyzed proximity labeling (PL), using the engineered promiscuous biotin ligase TurboID, as a sensitive method for characterizing PPIs in signaling networks. We show that TurboID fused with the GSK3-like kinase BIN2 or a PP2A phosphatase biotinylate their known substrate, the BZR1 transcription factor, with high specifically and efficiency. We optimized the protocol of biotin labeling and affinity purification in transgenic Arabidopsis expressing a BIN2-TurboID fusion protein. Subsequent quantitative mass spectrometry (MS) analysis identified about three hundred proteins biotinylated by BIN2-TurboID more efficiently than the YFP-TurboID control. These include a significant subset of previously proven BIN2 interactors and a large number of new BIN2 interactors that uncover a broad BIN2 signaling network. Our study illustrates that PL-MS using TurboID is a powerful tool for mapping signaling networks in plants, and reveals broad roles of this GSK3-like kinase in cellular signaling and regulation.
2023-05-10 | PXD017085 | Pride
Project description:In Arabidopsis thaliana, brassinosteroid (BR) signaling and stomatal development are connected through the SHAGGY/GSK3-like kinase BR INSENSITIVE2 (BIN2). BIN2 is a key negative regulator of BR signaling but it plays a dual role in stomatal development. BIN2 promotes or restricts stomatal asymmetric cell division (ACD) depending on its subcellular localization, which is regulated by the stomatal lineage-specific scaffold protein POLAR. BRs inactivate BIN2, but how they govern stomatal development remains unclear. Mapping the single-cell transcriptome of stomatal lineages after triggering BR signaling with either exogenous BRs or the specific BIN2 inhibitor, bikinin, revealed that the two modes of BR signaling activation generate spatiotemporally distinct transcriptional responses. We established that BIN2 is always sensitive to the inhibitor but, when in a complex with POLAR and its closest homolog POLAR-LIKE1, it becomes protected from BR-mediated inactivation. Subsequently, BR signaling in ACD precursors is attenuated, while it remains active in epidermal cells devoid of scaffolds and undergoing differentiation. Our study demonstrates how scaffold proteins contribute to cellular signal specificity of hormonal responses in plants.
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Project description:Malignant tumors, or cancers, are increasingly menacing people's life and health. For your female cancer patient, the ideal therapy should achieve dual purpose: suppress tumor progression meanwhile protect ovarian function. We previously showed that activated (phosphorylated) BIN2 in mouse ovaries regulates primordial follicle activation and oocyte quality through p-RPS6, and in this study, we found that BIN2 knockout or inhibition of BIN2 phosphorylation by BPP could suppress the genesis and progression of ovarian cancer. However, in human female ovarian cancer tissues, we didn’t see the increment of p-RPS6 although we observed a significant raise of p-BIN2. From this discrepancy between normal ovaries and ovarian cancer tissue, we guessed that p-BIN2 has other targets that are more important in ovarian cancer progression. Through mass spec identification, we found that only the constitutively active form of BIN2 (T423D & S424D) baits HDAC1, indicating that HDAC1 is a more important target of BIN2 in ovarian cancer. Next, we did saw Bin2 knockout or inhibition significantly decreased p-HDAC1 (S421) meanwhile increased H3K27ac. Moreover, chip seq showed that BIN2 inhibition significantly increased the binding of H3K27ac to multiple oncogenes. Besides, BIN2 knockout or inhibition could meanwhile protect ovarian function in mice with chemical carcinogen-induced in-situ ovarian cancers or with ovarian cancer cell transplantation. This study suggested that BIN2 inhibition could both suppress ovarian tumorigenesis and protect ovarian fertility, but through distinct mechanisms.
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Project description:Transcriptomic analysis of lignin mutants in Arabidopsis
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Project description:Malignant tumors, or cancers, are increasingly menacing people's life and health. For your female cancer patient, the ideal therapy should achieve dual purpose: suppress tumor progression meanwhile protect ovarian function. We previously showed that activated (phosphorylated) BIN2 in mouse ovaries regulates primordial follicle activation and oocyte quality through p-RPS6, and in this study, we found that BIN2 knockout or inhibition of BIN2 phosphorylation by BPP could suppress the genesis and progression of ovarian cancer. However, in human female ovarian cancer tissues, we didn’t see the increment of p-RPS6 although we observed a significant raise of p-BIN2. From this discrepancy between normal ovaries and ovarian cancer tissue, we guessed that p-BIN2 has other targets that are more important in ovarian cancer progression. Through mass spec identification, we found that only the constitutively active form of BIN2 (T423D & S424D) baits HDAC1, indicating that HDAC1 is a more important target of BIN2 in ovarian cancer. Next, we did saw Bin2 knockout or inhibition significantly decreased p-HDAC1 (S421) meanwhile increased H3K27ac. Moreover, chip seq showed that BIN2 inhibition significantly increased the binding of H3K27ac to multiple oncogenes. Besides, BIN2 knockout or inhibition could meanwhile protect ovarian function in mice with chemical carcinogen-induced in-situ ovarian cancers or with ovarian cancer cell transplantation. This study suggested that BIN2 inhibition could both suppress ovarian tumorigenesis and protect ovarian fertility, but through distinct mechanisms.
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Project description:Transcriptomic analysis on Brassinosteroid signaling mutants and activators in Arabidopsis
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