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Epidermal Growth Factor Receptor Maintains Cardiac Contractility Via Modulation of Protein Phosphatase 2A B' Regulatory Subunit PR72 Expression

ABSTRACT: Epidermal Growth Factor Receptor Maintains Cardiac Contractility Via Modulation of Protein Phosphatase 2A B' Regulatory Subunit PR72 Expression

PROVIDER: PRJNA589613 | ENA |

REPOSITORIES: ENA

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Catalytic Subunit of Protein Phosphatase 2A (PP2Ac) Influences the Meiosis Initiation During Spermatocyte Meiosis Prophase I

Project description:As a serine/threonine phosphatase, protein phosphatase 2A (PP2A) is essential in numerous physiological processes. Our previously study confirmed PP2A dysfunction can cause azoospermia by generating catalytic subunit of PP2A (Ppp2ca) conditional knockout (CKO) in C57BL/6J mice. Here, we further explored the possible mechanisms by focusing on meiosis initiation and spermatogenesis. The deficiency of Ppp2ca in germ cells conspicuously disturbed spermatogonial differentiation and lead to pachytene arrest, accompanied by defects in programmed double-strand break (DSB) repair and meiotic sex chromosome inactivation (MSCI). Furthermore, Ppp2ca-deficient spermatocytes exhibited abnormal agglutination and cohesion complex degradation of chromosome, probably contributing to pachytene arrest. Our study demonstrates the irreplaceable role of PP2A in spermatogenesis and provide more evidences on azoospermia etiology.

2021-12-01 | GSE181132 | GEO

Epidermal Growth Factor Receptor Maintains Cardiac Contractility Via Modulation of Protein Phosphatase 2A B' Regulatory Subunit PR72 Expression

Project description:To determine the differences of gene expression pattern in 7 and 9 weeks old cardiac EGFR KO mice versus control

2021-01-03 | GSE140407 | GEO

Sex-specific regulation of the cardiac transcriptome by the protein phosphatase 2A regulatory subunit B55α

Project description:Sex-specific regulation of the cardiac transcriptome by the protein phosphatase 2A regulatory subunit B55α

| PRJNA1105943 | ENA

Mapping the substrate landscape of protein phosphatase 2A catalytic subunit PPP2CA

Project description:Protein phosphatase 2A (PP2A) is an essential Ser/Thr phosphatase that regulates a plethora of cellular processes. PP2A operates as a holoenzyme complex, comprising one each of the scaffolding (A), regulatory (B) and catalytic (C) subunits. PPP2CA is the principal catalytic subunit of the PP2A holoenzyme complex. Although previous studies have reported many substrates of specific PP2A holoenzyme complexes, the full scope of PP2A substrates in cells remains to be defined. To address this, we generated HEK293 cells in which PPP2CA was homozygously knocked in with a dTAG, allowing for efficient and selective degradation of dTAG-PPP2CA with proteolysis-targeting chimeras (PROTACs) targeting the dTAG. By employing an unbiased global phospho-proteomic analysis, we identified 6,280 phospho-peptides corresponding to 2,204 proteins that showed a significant increase in abundance upon dTAG-PPP2CA degradation, implicating them as potential PPP2CA substrates. Among these, some were established PP2A substrates, while most were novel. Bioinformatic analyses revealed the involvement of the identified potential PPP2CA substrates in many cellular processes, including spliceosome function, the cell cycle, RNA transport and ubiquitin-mediated proteolysis. We show that a pSP/pTP motif is a predominant target for PPP2CA. We confirmed some of our phosphoproteomic data with immunoblotting, by utilising commercially available phospho-specific antibodies. We provide an in-depth atlas of potential PPP2CA substrates and establish targeted degradation as a robust tool to unveil phosphatase substrates in cells.

2024-03-18 | PXD045779 | Pride

Catalytic Subunit of Protein Phosphatase 2A (PP2Ac) Influences the Meiosis Initiation During Spermatocyte Meiosis Prophase I

Project description:Catalytic Subunit of Protein Phosphatase 2A (PP2Ac) Influences the Meiosis Initiation During Spermatocyte Meiosis Prophase I

| PRJNA750761 | ENA

Unmasking of Protein Phosphatase 2 Regulatory Subunit B as a crucial factor in the development and progression of dilated cardiomyopathy

Project description:The PPP2R5D encodes for a Protein phosphatase 2A (PP2A), one of the four major Ser/Thr phosphatases negatively controlling cell growth and division. PP2A is consisting of a common heteromeric core enzyme with a catalytic subunit and a B regulatory subunit that might control the substrate selectivity and catalytic activity. We investigated the potential role of Ppp2r5d for the cardiomyocyte (cultured mouse cardiomyocytes).

2024-09-30 | GSE238141 | GEO

Sex-specific regulation of the cardiac transcriptome by the protein phosphatase 2A regulatory subunit B55α

Project description:Protein phosphatase 2A (PP2A) enzymes containing the regulatory subunit isoform B55α (PP2A-B55α) suppress HDAC5/MEF2 signalling in cardiac myocytes, implicating B55α in the transcriptional regulation of cardiac growth and fibrosis. The role of B55α in the heart has not been investigated. In this study, we generated and characterised two loss-of-function mouse models, with global or cardiomyocyte-specific disruption of the gene encoding B55α (Ppp2r2a). Mice with global homozygous knockout of B55α died in utero, but cardiac morphology was unremarkable compared with wildtype littermates. Mice with global heterozygous knockout of B55α had thinner left ventricular walls compared with wildtype mice at 12 months of age, an effect that was more pronounced in males. Mice with cardiomyocyte-specific deletion of B55α displayed normal cardiac morphology at 10-12 weeks of age, demonstrating that cardiomyocyte B55α is not required for postnatal heart growth. Despite no obvious morphological differences, gene expression analyses revealed extensive remodelling of the cardiac transcriptome in male, but not female, mice. In males, B55α knockout increased the expression of genes associated with extracellular matrix composition, and downregulated genes associated with mitochondrial energy production. This study reveals a sexually dimorphic role for B55α in postnatal cardiac transcriptional regulation and provides a foundation for future work investigating the role of B55α in cardiac stress settings.

2024-05-05 | GSE266131 | GEO

Integrator Recruits Protein Phosphatase 2A to Prevent Pause Release and Enable Transcription Termination

Project description:Efficient release of promoter-proximally paused Pol II into productive elongation is essential for gene expression. Recently, we reported that the Integrator complex can bind paused Pol II and drive premature transcription termination, potently attenuating the activity of target genes. Premature termination requires RNA cleavage by the endonuclease subunit of Integrator, but the roles of other Integrator subunits in gene regulation have yet to be elucidated. Here, we report that Integrator subunit 8 (IntS8) is critical for transcription repression through its association with Protein Phosphatase 2A (PP2A). We find that Integrator-bound PP2A dephosphorylates the Pol II C-terminal domain and Spt5, and prevents the transition to productive elongation. Blocking PP2A association with Integrator thus stimulates pause release and gene activation. These results reveal a second catalytic function associated with Integrator-mediated transcription termination, and suggest a new model for the control of productive elongation involving active competition between transcriptional kinases and phosphatases.

2020-10-06 | GSE150844 | GEO

Protein phosphatase 2A activation promotes heart transplant acceptance in mice

Project description:Protein phosphatase 2A activation promotes heart transplant acceptance in mice

| PRJNA989246 | ENA

Protein phosphatase 2A protects centromeric sister chromatid cohesion during meiosis I

Project description:Segregation of homologous maternal and paternal centromeres to opposite poles during meiosis I depends on post-replicative crossing over between homologous non-sister chromatids, which creates chiasmata and therefore bivalent chromosomes. Destruction of sister chromatid cohesion along chromosome arms due to proteolytic cleavage of cohesin's Rec8 subunit by separase resolves chiasmata and thereby triggers the first meiotic division. This produces univalent chromosomes, the chromatids of which are held together by centromeric cohesin that has been protected from separase by shugoshin (Sgo1/MEI-S332) proteins. Here we show in both fission and budding yeast that Sgo1 recruits to centromeres a specific form of protein phosphatase 2A (PP2A). Its inactivation causes loss of centromeric cohesin at anaphase I and random segregation of sister centromeres at the second meiotic division. Artificial recruitment of PP2A to chromosome arms prevents Rec8 phosphorylation and hinders resolution of chiasmata. Our data are consistent with the notion that efficient cleavage of Rec8 requires phosphorylation of cohesin and that this is blocked by PP2A at meiosis I centromeres. Keywords: ChIP-chip, Mitosis, Meiosis, Cell cycle, Saccharomyces cerevisiae, Chromosome VI tiling array, Sgo1, Pp2A, Cse4, Ndc10, Rts1, Rec8

2006-05-10 | GSE4791 | GEO

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