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Transcriptome analysis of females and males following knockdown serine/threonine protein phosphatase 1 catalytic subunit encoding genes(Sj-pp1c) in Schistosoma japonicum

ABSTRACT: Transcriptome analysis of females and males following knockdown serine/threonine protein phosphatase 1 catalytic subunit encoding genes(Sj-pp1c) in Schistosoma japonicum

PROVIDER: PRJNA428455 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR6439810_1.fastq.gz	Fastqsanger.gz
	SRR6439810_2.fastq.gz	Fastqsanger.gz
	SRR6439811_1.fastq.gz	Fastqsanger.gz
	SRR6439811_2.fastq.gz	Fastqsanger.gz
	SRR6439812_1.fastq.gz	Fastqsanger.gz

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Transcriptome analysis of females and males following knockdown serine/threonine protein phosphatase 1 catalytic subunit encoding genes(Sj-pp1c) in Schistosoma japonicum

Project description:Purpose: To obtain the differentially expressed genes based on post-RNAi transcriptional profiling analysis of females and males, which provide a more comprehensive overview about the effects of Sj-pp1c knockdown on schistosoma developmental and reproduction biology at the molecular level. Methods: Schistosoma japonicum females and males were collected from 21 days post infection worm pairs that untreated (Blank,BLA_FE/M) or treated with combined Sj-pp1c dsRNAs (Sj-pp1c KD,PP1_FE/M) cultured for 7 d in vitro. Total mRNA profiles of females and males were generated by deep sequencing, in triplicate, using Illumina HiSeqTM2000. Results: 41-51 million reads (average 44 million) were obtained for each sample after quality filtering, and 63-67% reads were mapped to S. japonicum reference genome(WormBase ParaSite, http://parasite.wormbase.org/ftp.html; version 7.0) and identified 15,314 transcripts by Tophat (version v2.0.12) and Cufflinks (Version 2.1.1.). 2291 and 229 transcripts showed differentially expressed in males and females, respectively,between the untreated and Sj-pp1c dsRNAs treated group, with adjust P value <0.05. GO analysis showed differentially expressed genes are mainly function in extracellular matrix structural constituent, proteolysis and collagen trimer. Conclusions: We performed analysis on transcriptional profiling of females and males following Sj-pp1c-RNAi by RNA-seq, which provided molecular evidence for the pleiotropic roles that Sj-pp1c plays in schistosome biology.

2018-06-24 | GSE108738 | GEO

Serine/Threonine phosphatase PP2A is essential for optimal B cell function

Project description:Protein phosphatase 2A (PP2A), a serine/threonine phosphatase, has been shown to control T cell function. We found that in vitro activated B cells and B cells from various lupus-prone mice and patients with systemic lupus erythematosus display increased PP2A activity. To understand the contribution of PP2A to B cell function, we generated a Cd19CrePpp2r1aflox/flox (flox/flox) mouse which lacks functional PP2A only in B cells. Flox/flox mice displayed reduced spontaneous germinal center formation and decreased responses to T-dependent and T-independent antigens while their B cells responded poorly in vitro to stimulation with an anti-CD40 antibody or CpG in the presence of IL-4. Transcriptome and metabolome studies revealed altered NAD and purine/pyrimidine metabolism and increased expression of purine nucleoside phosphorylase in PP2A-deficient B cells. Our results demonstrate that PP2A is required for optimal B cell function and may contribute to increased B cell activity in systemic autoimmunity.

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Serine/Threonine phosphatase PP2A is essential for optimal B cell function

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Mitochondrial phosphoglycerate mutase 5 uses alternate catalytic activity as a protein serine/threonine phosphatase to activate ASK1.

Project description:Phosphoglycerate mutase (PGAM) is an enzyme of intermediary metabolism that converts 3-phosphoglycerate to 2-phosphoglycerate in glycolysis. Here, we discovered PGAM5 that is anchored in the mitochondrial membrane lacks PGAM activity and instead associates with the MAP kinase kinase kinase ASK1 and acts as a specific protein Ser/Thr phosphatase that activates ASK1 by dephosphorylation of inhibitory sites. Mutation of an active site His-105 in PGAM5 abolished phosphatase activity with ASK1 and phospho-Thr peptides as substrates. The Drosophila and Caenorhabditis elegans orthologs of PGAM5 also exhibit specific Ser/Thr phosphatase activity and activate the corresponding Drosophila and C. elegans ASK1 kinases. PGAM5 is unrelated to the other known Ser/Thr phosphatases of the PPP, MPP, and FCP families, and our results suggest that this member of the PGAM family has crossed over from small molecules to protein substrates and been adapted to serve as a specialized activator of ASK1.

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Project description:While the importance of cellular and viral kinases in HCMV replication has been demonstrated, relatively little is known about the activity of cellular phosphatases. We conducted a series of experiments designed to investigate the effect of HCMV infection on cellular serine/threonine phosphatase activity. We found that the abundance of two major cellular serine/threonine phosphatases, PP1 and PP2A, increases during HCMV infection. This was associated with an increase in threonine phosphatase activity in HCMV-infected cells. HCMV infection conferred resistance to the effects of the phosphatase inhibitors calyculin A (CA) and okadaic acid with regards to global protein hyperphosphorylation and the shutoff of protein synthesis. The protective effect of HCMV infection could be overcome at a high concentration of CA, suggesting that cellular phosphatase activity is required for critical cellular processes during HCMV infection. Specifically, phosphatase activity was required to limit the accumulation of phospho-eIF2alpha, but not phospho-PKR, during HCMV infection.

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