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Deletion of conserved protein phosphatases reverses defects associated with mitochondrial DNA damage in Saccharomyces cerevisiae

ABSTRACT: Mitochondrial biogenesis is regulated by signaling pathways sensitive to extracellular conditions and to the internal environment of the cell. We found that deletion of protein phosphatase 2A (PP2A) or of protein phosphatase 6 (PP6) diminishes the nuclear transcriptional response associated with mtDNA damage.

ORGANISM(S): Saccharomyces cerevisiae

PROVIDER: GSE52242 | GEO | 2013/12/23

SECONDARY ACCESSION(S): PRJNA227236

REPOSITORIES: GEO

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Deletion of conserved protein phosphatases reverses defects associated with mitochondrial DNA damage in Saccharomyces cerevisiae

Project description:Mitochondrial biogenesis is regulated by signaling pathways sensitive to extracellular conditions and to the internal environment of the cell. We found that deletion of protein phosphatase 2A (PP2A) or of protein phosphatase 6 (PP6) diminishes the nuclear transcriptional response associated with mtDNA damage. Six samples were analyzed to determine message RNA levels.

2013-12-23 | E-GEOD-52242 | biostudies-arrayexpress

Siginificance of Saccharomyces cerevisiae Cdc55p on gene expression at initial stage of alcoholic fermentation

Project description:Our previous report revealed that protein phosphatase 2A (PP2A), complexed with the B55delta-type regulatory subunit (i.e. Cdc55p), is solely responsible for the outstanding glycolytic activity of sake yeast strains (Watanabe et al., Appl. Environ. Microbiol. 85, e02083-18 (2019). However, how PP2A mediates yeast alcoholic fermentation remains elusive. Thus, RNA-seq analysis of S. cerevisiae cdc55-delta cells at the initial fermentation stage was performed to identify the downstream effector targeting the glycolytic control.

2023-08-08 | GSE220072 | GEO

Deletion of conserved protein phosphatases reverses defects associated with mitochondrial DNA damage in Saccharomyces cerevisiae.

Project description: Not available

| S-EPMC3910629 | biostudies-literature

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

Integrator-PP2A complex dephosphorylates the C-terminal repeat domain of RNA Polymerase II

Project description:The phosphorylation and dephosphorylation of transcription machinery are essential for the precise control of gene expression. A non-canonical protein phosphatase 2A (PP2A) holoenzyme (denoted INTAC), in which the 14-subunit Integrator recruits RNA polymerase II (Pol II) and the PP2A core enzyme dephosphorylates the C-terminal repeat domain (CTD) of Pol II at Serine-5 and Serine-2.

2020-12-02 | GSE154093 | GEO

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

Regulation of PP2A-subfamily holoenzyme function by carboxyl-terminal methylation

Project description:The family of Phosphoprotein Phosphatases (PPPs) is responsible for most cellular serine and threonine dephosphorylation. PPPs achieve substrate specificity and selectivity by forming multimeric holoenzymes with catalytic, scaffolding, and regulatory subunits. Although there are only ten catalytic PPP subunits encoded in the human genome, the formation of holoenzymes creates hundreds of unique enzymes that oppose kinases and carry out specific dephosphorylation reactions. Thus, to achieve the correct cellular phosphorylation state, the assembly of PPP holoenzymes needs to be tightly controlled. Indeed, changes in the cellular repertoire of PPPs are frequently linked to human disease, including cancer and neurodegeneration. The Protein Phosphatase 2A (PP2A) subfamily of PPPs consists of PP2A, PP4, PP6, and holoenzyme formation is at least in part regulated by carboxyl (C)-terminal methyl-esterification (often referred to as methylation) of the catalytic subunits. This reversible modification is catalyzed by a Leucine Carboxyl Methyltransferase-1 (LCMT1) that utilizes S-adenosyl-methionine (SAM) as the methyl donor and removed by Protein Phosphatase Methylesterase 1 (PME1). For PP2A, C-terminal methylation controls regulatory subunit selection. Notably, different types of regulatory subunits display differential methylation sensitivity. For PP4 and PP6, the role of C-terminal methylation is less well defined. Here, we use mass spectrometry-based proteomics, methylation-ablating mutations, and genome editing to comprehensively elucidate the role of C-terminal methylation in PP2A, PP4, and PP6 function in multiple cell lines. Using these approaches, we quantitatively determine the effects of reduced C-terminal methylation on PP2A, PP4, and PP6 holoenzyme assembly in an unbiased, isoform-specific manner.

| MSV000086183 | MassIVE

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.

2020-02-04 | GSE144700 | GEO

PP2A dependent modulation of c-Myc and p21 leads to differentiation and cell cycle control in Acute Myeloid Leukemia

Project description:Aberrant kinase and phosphatase activity frequently contribute to Acute Myeloid Leukemia. Here we characterize the Protein Phosphatase 2A (PP2A) as a mediator of differentiation and cell cycle arrest in AML. Using a novel PP2A activator OSU-2S, we show that PP2A activation results in differentiation, growth arrest and cell death in AML, via depletion of c-Myc and upregulation of p21. Gene expression and mass cytometric profiling further show modulation of cell cycle regulators and differentiation factors, and importantly, decreased CD34+/CD38- stem cells in patient derived AML blasts treated with OSU-2S. Finally, we demonstrate in-vivo therapeutic efficacy of OSU-2S as seen by increased differentiation, decreased clonogenicity and improved survival in a Tet2-/-Flt3ITD murine AML model and human AML models.

2022-03-16 | GSE148018 | GEO

MDAMB-231 Fusion Lumos, LC-MSMS

Project description:The protein phosphatase 2A (PP2A) heterotrimer PP2A-B56A is a human tumor suppressor. However, the molecular mechanisms inhibiting PP2A-B56A in cancer are poorly understood. Here, we report Phosphoproteomics study of single point mutation of CIP2A(K21A) in triple negative breast cancer cell line (MDA-MB-231).

2022-10-21 | PXD035179 | Pride

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