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DEG9, a serine protease modulates cytokinins and light signaling by regulating the level of Arabidopsis Response Regulator 4

ABSTRACT: DEG9, a serine protease modulates cytokinins and light signaling by regulating the level of Arabidopsis Response Regulator 4

PROVIDER: PRJEB14331 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	ERR1447790.fastq.gz	Fastqsanger.gz
	ERR1447791.fastq.gz	Fastqsanger.gz
	ERR1447792.fastq.gz	Fastqsanger.gz
	ERR1447793.fastq.gz	Fastqsanger.gz
	ERR1447794.fastq.gz	Fastqsanger.gz

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DEG9, a serine protease modulates cytokinins and light signaling by regulating the level of Arabidopsis Response Regulator 4

Project description:The Arabidopsis seedlings treated with 2M t-zeatin (CTK) for 30 minutes and then total RNA was extracted from Arabidopsis seedlings using TRIzol reagent (Invitrogen) and treated with RNase-free DNase I. The poly(A) mRNA was isolated using oligo (dT) beads. First-strand cDNA was subsequently generated using random hexamer-primed reverse transcription, followed by synthesis of the second-strand cDNA using RNaseH and DNA polymerase I. Then, single-end and paired-end RNA-seq libraries were prepared following Illumina's protocols and sequenced on the Illumina GA II platform.

2016-06-17 | E-MTAB-4603 | biostudies-arrayexpress

DEG9, a serine protease, modulates cytokinin and light signaling by regulating the level of ARABIDOPSIS RESPONSE REGULATOR 4.

Project description:Cytokinin is an essential phytohormone that controls various biological processes in plants. A number of response regulators are known to be important for cytokinin signal transduction. ARABIDOPSIS RESPONSE REGULATOR 4 (ARR4) mediates the cross-talk between light and cytokinin signaling through modulation of the activity of phytochrome B. However, the mechanism that regulates the activity and stability of ARR4 is unknown. Here we identify an ATP-independent serine protease, degradation of periplasmic proteins 9 (DEG9), which localizes to the nucleus and regulates the stability of ARR4. Biochemical evidence shows that DEG9 interacts with ARR4, thereby targeting ARR4 for degradation, which suggests that DEG9 regulates the stability of ARR4. Moreover, genetic evidence shows that DEG9 acts upstream of ARR4 and regulates the activity of ARR4 in cytokinin and light-signaling pathways. This study thus identifies a role for a ubiquitin-independent selective protein proteolysis in the regulation of the stability of plant signaling components.

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Knockdown of serine protease PRSS23 decreased FGF2 expression in gastric cancer

Project description:Serine proteases dysregulation has been considered to be closely associated with the inflammatory response and tumor progression. As a novel serine protease, the biological function of PRSS23 is rarely studied in cancers. In this study, we explored the biological function of PRSS23 in GC by RNA sequencing. Our data highlights that PRSS23 promotes GC progression by promoting macrophage infiltration via regulating FGF2 expression.

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Knockdown of serine protease PRSS23 decreased FGF2 expression in gastric cancer

Project description:Knockdown of serine protease PRSS23 decreased FGF2 expression in gastric cancer

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Serine protease NAL1 exerts pleiotropic functions through degradation of TOPLESS-related corepressor in rice

Project description:Serine protease NAL1 exerts pleiotropic functions through degradation of TOPLESS-related corepressor in rice

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Serine protease NAL1 exerts pleiotropic functions through degradation of TOPLESS-related corepressor in rice

Project description:NAL1 (NARROW LEAF 1) is a breeding-valuable pleiotropic gene that affects multiple agronomic traits in rice, but the molecular mechanism is largely unclear. Here, we report that NAL1 is a serine protease and displays a novel hexameric structure whose formation is mediated by ATP-containing positively charged pocket at the N-terminal region. Moreover, we identified TOPLESS-related corepressor OsTPR2 involved in multiple growth and development processes as the substrate of NAL1. We found that NAL1 degraded OsTPR2, thus modulating the expression of downstream genes related to hormone signaling pathways, eventually achieving its pleiotropic physiological function. An elite allele NAL1A originated from wild rice could increase grain yield. Furthermore, the NAL1 homologs in different crops have a similar pleiotropic function to NAL1. Our study uncovers a NAL1-OsTPR2 regulatory module and provides gene resources for the design of high-yield crops.

2023-05-09 | GSE207132 | GEO

Serine protease HtrA1 modulates chemotherapy-induced cytotoxicity.

Project description:Resistance to chemotherapy presents a serious challenge in the successful treatment of various cancers and is mainly responsible for mortality associated with disseminated cancers. Here we show that expression of HtrA1, which is frequently downregulated in ovarian cancer, influences tumor response to chemotherapy by modulating chemotherapy-induced cytotoxicity. Downregulation of HtrA1 attenuated cisplatin- and paclitaxel-induced cytotoxicity, while forced expression of HtrA1 enhanced cisplatin- and paclitaxel-induced cytotoxicity. HtrA1 expression was upregulated by both cisplatin and paclitaxel treatment. This upregulation resulted in limited autoproteolysis and activation of HtrA1. Active HtrA1 induces cell death in a serine protease-dependent manner. The potential role of HtrA1 as a predictive factor of clinical response to chemotherapy was assessed in both ovarian and gastric cancer patients receiving cisplatin-based regimens. Patients with ovarian or gastric tumors expressing higher levels of HtrA1 showed a higher response rate compared with those with lower levels of HtrA1 expression. These findings uncover what we believe to be a novel pathway by which serine protease HtrA1 mediates paclitaxel- and cisplatin-induced cytotoxicity and suggest that loss of HtrA1 in ovarian and gastric cancers may contribute to in vivo chemoresistance.

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Serine Metabolism Orchestrates Macrophage Polarization by Regulating the IGF1–p38 Axis

Project description:Here we show that suppressing the serine biosynthesis pathway, either by inhibiting the activity of the key enzyme phosphoglycerate dehydrogenase or by exogenous serine and glycine restriction, robustly enhances polarization of interferon-g-activated macrophages (M(IFN-g)) but suppresses that of interleukin-4-activated macrophages (M(IL-4)) both in vitro and in vivo.To further explore its mechanism, we used high-throughput sequencing technology (RNA-seq) to assess gene expression in serine-deficiency or not BMDMs

2022-02-19 | GSE196840 | GEO

Protease Treatment

Project description:Determine if transcripts are released by protease treatment Keywords: Comparison of protease treatments

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Transmembrane serine protease 2 and proteolytic activation of the epithelial sodium channel in mouse kidney: Early effects of aldosterone

Project description:The appropriate regulation of the epithelial sodium channel (ENaC) in the aldosterone-sensitive distal nephron is required for sodium homeostasis and thereby for the long-term regulation of arterial blood pressure. A unique feature of ENaC is its activation by proteolytic cleavage. However, the relevant proteases involved in proteolytic ENaC activation in the kidney remain elusive. Here, we examined a potential role of transmembrane serine protease 2 (TMPRSS2). A mouse cortical collecting duct cell line (mCCDcl1) was used as a model system. We performed RNA-Seq transcriptome analysis of mCCDcl1 cells, which confirmed coexpression of Tmprss2 and all three ENaC subunits (Scnn1a, Scnn1b, Scnn1g) in this cell line. Importantly, high baseline expression of TMPRSS2 was detected in these cells without a stimulatory effect of aldosterone on its function or transcription. TMPRSS2 knockout in mCCDcl1 cells compromised γ-ENaC cleavage and reduced baseline and aldosterone-stimulated transepithelial short-circuit currents, which could be rescued by chymotrypsin. A compensatory transcriptional upregulation of other proteases was not observed. From these findings we conclude that TMPRSS2 is likely to contribute to proteolytic ENaC activation in the kidney.

2024-10-30 | GSE274304 | GEO

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