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CAMP/PKA signaling balances respiratory activity with mitochondria dependent apoptosis via transcriptional regulation

ABSTRACT: This data provides evidence that elevation of cAMP levels has a dramatic effect on the transcriptome of yeast cells, with particular emphasis on mitochondrial function and the promotion of ROS production

ORGANISM(S): Schizosaccharomyces pombe Saccharomyces cerevisiae

PROVIDER: GSE25541 | GEO | 2010/11/24

SECONDARY ACCESSION(S): PRJNA134017

REPOSITORIES: GEO

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cAMP/PKA signaling balances respiratory activity with mitochondria dependent apoptosis via transcriptional regulation

Project description:This data provides evidence that elevation of cAMP levels has a dramatic effect on the transcriptome of yeast cells, with particular emphasis on mitochondrial function and the promotion of ROS production S. cerevisiae cells lacking the high affinity phosphodiesterase PDE2or both PDE2 and the PKA subunit TPK3 were grown for 24h in rich media in the presence of 4mM exogensously added cAMP. 8 samples.

2010-11-24 | E-GEOD-25541 | biostudies-arrayexpress

cAMP/PKA signaling balances respiratory activity with mitochondria dependent apoptosis via transcriptional regulation.

Project description: Not available

| S-EPMC3001716 | biostudies-literature

MiR-221/222 suppression induced by activation of the cAMP/PKA/CREB1 pathway is required for cAMP-induced bidirectional differentiation of glioma cells [miRNA]

Project description:Factors that increase cAMP levels can induce lineage-specific differentiation of glioma cells into astrocyte-like cells. However, the differentiation pattern and underlying mechanisms remain unclear. Here, we find that cAMP/PKA/CREB1-induced miR-221/222 suppression contributes to the neuron-like differentiation of gliomas. cAMP agonists selectively induced neuron- and astrocyte-like but not oligodendrocyte-like differentiation of C6 glioma cells. PKA inhibitors and CREB1 knockout blocked neuron-like differentiation of glioma cells. cAMP inhibited miR-221/222 in a PKA/CREB1 dependent manner. Importantly, both in vitro and in vivo assays demonstrated that transcriptional suppression of miR-221/222 is required for neuronal differentiation of glioma cells. Our findings suggest that increasing cAMP levels can induce bidirectional differentiation of glioma cells. Furthermore, the miR-221/222 cluster acts as an epigenetic brake during glioma differentiation. Factors that increase cAMP levels can induce lineage-specific differentiation of glioma cells into astrocyte-like cells. However, the differentiation pattern and underlying mechanisms remain unclear. Here, we find that cAMP/PKA/CREB1-induced miR-221/222 suppression contributes to the neuron-like differentiation of gliomas. cAMP agonists selectively induced neuron- and astrocyte-like but not oligodendrocyte-like differentiation of C6 glioma cells. PKA inhibitors and CREB1 knockout blocked neuron-like differentiation of glioma cells. cAMP inhibited miR-221/222 in a PKA/CREB1 dependent manner. Importantly, both in vitro and in vivo assays demonstrated that transcriptional suppression of miR-221/222 is required for neuronal differentiation of glioma cells. Our findings suggest that increasing cAMP levels can induce bidirectional differentiation of glioma cells. Furthermore, the miR-221/222 cluster acts as an epigenetic brake during glioma differentiation.

2021-08-24 | GSE182498 | GEO

Expression data from BeWo cells treated without or with PKA- or EPAC-selected cAMP analogs

Project description:Cyclic AMP activates two downstream factors, protein kinase A (PKA) and exchange protein directly activated by cAMP (EPAC) and both downstream signalings induce syncytialization, cell fusion and the production of hCG and progesterone. We used microarray to identify novel transcription factors related to syncytialization in two cAMP signaling-stimulated BeWo cells.

2017-09-30 | GSE100095 | GEO

Effect of Cold Atmospheric Microwave Plasma (CAMP) on wound healing in canine keratinocytes

Project description:CAMP treatment provided beneficial effects for the curative wound process through induction of genes involved in wound healing, promotion of EMT, and increase of the molecular targets in the hippo signaling pathway.

2023-01-17 | GSE222898 | GEO

cAMP/PKA signaling promotes AKT deactivation via reducing CIP2A expression, thereby facilitating decidualization

Project description:Decidualization is a progesterone-initiated differentiation concerning the endometrium and is dedicated to supporting the placenta and embryo development. During the process, cAMP signaling is widely known to be indispensable, but the details are not fully understood. In this study, we show that cAMP signaling promotes AKT deactivation in endometrial stromal cells, which favors their decidualization. The deactivation of AKT is found to be a consequence of the reduced expression of several inhibitors of PP2A, the major phosphatase of AKT, with CIP2A being the most prominent. To show that CIP2A loss is obligatory for decidualization, we performed this ATAC-seq analysis. Persistent CIP2A expression impairs the chromatin accesibility remodeling during decidualization.

2023-02-06 | GSE224212 | GEO

The cAMP-PKA signaling pathway regulates hyphal growth, conidiation, trap morphogenesis, stress tolerance and autophagy in Arthrobotrys oligospora

Project description:Signal transduction plays a crucial role in defending against external environmental challenges, which can modulate the cellular response to external stimuli. cAMP/PKA signaling pathway is one of the most important signaling circuits and is evolutionarily conserved in eukaryotes. A. oligospora is a typical nematode-trapping fungi that can specialize adhesive network traps to kill nematodes after sensing the signals. To elucidate the biological roles of cAMP-PKA signaling pathway, we characterized an adenylate cyclase orthologous protein, AoAcy, a cAMP-dependent protein kinase regulator, AoPKaR, and two cAMP-dependent protein kinase catalytic subunits, AoPKaCs in A. oligospora. Furthermore, phenotypic analysis of the gene disruption strains showed that the deletion of AoAcy resulted in a significant decrease in the content of cAMP and arthrobotrisins, and the results indicated that AoAcy, AoPKaR and AoPKaC1 were involved in the hyphae growth, trap morphogenesis, sporulation, stress resistance and autophagy. In addition, AoAcy and AoPKaC1 were also participated in the regulation of mitochondria, thereby affecting energy metabolism. While AoPKaC2 only affected sporulation, the number of nuclei and autophagy. Collectively, these findings highlight the essential role of cAMP/PKA signaling pathway in A. oligospora and provide insights into the regulation mechanisms of signaling pathways in trap formation and sporulation.

2022-08-13 | GSE210886 | GEO

cAMP/PKA signaling phosphorylates LRBA in renal collecting duct

Project description:Vasopressin/cAMP/protein kinase A (PKA)/aquaporin-2 (AQP2) water channels signaling in the kidneys is a canonical pathway that determines AQP2 activity in response to body fluid balance. AQP2 phosphorylation by PKA increases water reabsorption from urine for the prevention of further water loss. We used several activators of cAMP/PKA signaling as screening tools to generate various phosphorylation patterns of PKA substrates and AQP2 in a mouse cortical collecting duct principal cell line (mpkCCDcl4). We next quantified phosphorylation levels of PKA substrates and AQP2 after western blot analysis using a phospho-PKA substrates antibody. Finally, we screen for PKA substrates whose phosphorylation levels were well correlated with those of AQP2. Immunoprecipitation with a phospho-PKA substrates antibody followed by mass spectrometry analysis revealed that the leading candidate in this assay proved to be a lipopolysaccharide-responsive and beige-like anchor protein (LRBA). Phosphorylation levels of LRBA was nearly perfectly correlated with those of AQP2.

2022-07-23 | PXD033852 | Pride

Redox control of the cAMP/PKA pathway during protein misfolding stress

Project description:Redox control of the cAMP/PKA pathway during protein misfolding stress

| PRJEB39415 | ENA

CaMKK2 Inactivation by cAMP-PKA Signaling and 14-3-3 Adaptor Proteins

Project description:The calcium-calmodulin (Ca2+-CaM) dependent protein kinase kinase-2 (CaMKK2) is activated by increases in intracellular Ca2+ and is a key regulator of cellular and wholebody energy metabolism. CaMKK2 inhibition protects against prostate cancer, hepatocellular carcinoma and metabolic derangements induced by a high-fat diet, therefore elucidating the intracellular mechanisms that inactivate CaMKK2 has important therapeutic implications. Here we show that stimulation of cyclic AMP (cAMP)-dependent protein kinase (PKA) signaling in cells inactivates CaMKK2 by phosphorylation of three conserved serine residues. PKA-dependent phosphorylation of Ser495 directly impairs Ca2+-CaM activation, whereas phosphorylation of Ser100 and Ser511 mediate recruitment of 14-3-3 adaptor proteins that hold CaMKK2 in the inactivated state by preventing dephosphorylation of phospho-Ser495. We also report the crystal structure of 14-3-3z bound to a synthetic diphosphorylated peptide that reveals how the canonical (Ser511) and non-canonical (Ser100) 14-3-3 consensus sites on CaMKK2 co-operate to bind 14-3-3 proteins. Our findings provide a detailed mechanistic insight into how cAMP-PKA signaling inactivates CaMKK2 and reveals a pathway to inhibit CaMKK2 with potential for treating human diseases.

2020-11-06 | PXD020133 | Pride

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