Cdc14 as transcription regulator of RNA pol-II
Ontology highlight
ABSTRACT:
ORGANISM(S): Saccharomyces cerevisiae
PROVIDER: GSE31020 | GEO | 2011/07/29
SECONDARY ACCESSION(S): PRJNA144921
REPOSITORIES: GEO
Similar Datasets
Project description:In yeast, the phosphatase Cdc14 is required for mitotic exit and for segregation of repetitive regions. Cdc14 is also a subunit of the silencing complex RENT, but no roles in transcription repression have been described. Here we report that Cdc14 promotes silencing at the integenic spacer sequences (IGS) of ribosomal genes during interphase and at Y' repeats in sub-telomeric regions during mitosis, through its ability to dephosphotylate the CDT domain of the RNA polymerase II. CDC14 and CDC15 strains were grown at 25°C and 37°C. Comparisons were made between each strain at different temperatures, and between strains at the same temperature.
2011-07-28 | E-GEOD-31020 | biostudies-arrayexpress
Project description:Transcriptome profiling of cdc14-3 and cdc14-3_snf1 mutants at non-permissive temp (35C) for 90min or 2hr followed by 30min NaCl stress. The experiment showed the aberrant cell cycle induction in cdc14-3 mutants upon NaCl response is abrogated with snf1 deletion in cdc14-3 background.
2014-12-03 | GSE56995 | GEO
Project description:CDC14 phosphatases are critical components of the cell cycle machinery that drives exit from mitosis in yeast. However, the two mammalian paralogs, CDC14A and CDC14B, are dispensable for cell cycle progression or exit, and their function remains unclear. By generating a double Cdc14a; Cdc14b -null mouse model, we report here that CDC14 phosphatases control cell differentiation in pluripotent cells, and their absence results in deficient development of the neural system. Lack of CDC14 impairs neural differentiation from embryonic stem cells (ESCs) accompanied by deficient induction of genes controlled by bivalent promoters. CDC14 directly dephosphorylates and destabilizes Undifferentiated embryonic Transcription Factor 1 (UTF1) during the exit from stemness. Multiomic single-cell analysis of differentiating ESCs suggest that increased UTF1 levels in the absence of CDC14 prevent the firing of bivalent promoters required for differentiation. These results, along recent data suggesting a critical role for cell cycle kinases in pluripotency, suggest that cell cycle kinase-phosphatase modules such as CDK-CDC14 are critical for linking cell cycle regulation and self-renewal, with a specific function for CDC14 phosphatases modulating key epigenetic regulators during the terminal exit from pluripotency.
2022-10-31 | GSE196139 | GEO
Project description:CDC14 phosphatases are critical components of the cell cycle machinery that drives exit from mitosis in yeast. However, the two mammalian paralogs, CDC14A and CDC14B, are dispensable for cell cycle progression or exit, and their function remains unclear. By generating a double Cdc14a; Cdc14b-null mouse model, we report here that CDC14 phosphatases control cell differentiation in pluripotent cells and their absence results in deficient development of the neural system. Lack of CDC14 impairs neural differentiation from embryonic stem cells (ESCs) accompanied by deficient induction of genes controlled by bivalent promoters. During ESC differentiation, CDC14 directly dephosphorylates and destabilizes Undifferentiated embryonic Transcription Factor 1 (UTF1), a critical regulator of stemness. In the absence of CDC14, increased UTF1 levels prevent the firing of bivalent promoters, resulting in defective induction of the transcriptional programs required for differentiation. These results suggest that mammalian CDC14 phosphatases function during the terminal exit from the cell cycle by modulating the transition from the pluripotent to the differentiated chromatin state, at least partially by controlling chromatin dynamics and transcription in a UTF1-dependent manner.
2022-10-31 | GSE191197 | GEO
Project description:CDC14 phosphatases are critical components of the cell cycle machinery that drives exit from mitosis in yeast. However, the two mammalian paralogs, CDC14A and CDC14B, are dispensable for cell cycle progression or exit, and their function remains unclear. By generating a double Cdc14a; Cdc14b -null mouse model, we report here that CDC14 phosphatases control cell differentiation in pluripotent cells, and their absence results in deficient development of the neural system. Lack of CDC14 impairs neural differentiation from embryonic stem cells (ESCs) accompanied by deficient induction of genes controlled by bivalent promoters. CDC14 directly dephosphorylates and destabilizes Undifferentiated embryonic Transcription Factor 1 (UTF1) during the exit from stemness. Multiomic single-cell analysis of differentiating ESCs suggest that increased UTF1 levels in the absence of CDC14 prevent the firing of bivalent promoters required for differentiation. These results, along recent data suggesting a critical role for cell cycle kinases in pluripotency, suggest that cell cycle kinase-phosphatase modules such as CDK-CDC14 are critical for linking cell cycle regulation and self-renewal, with a specific function for CDC14 phosphatases modulating key epigenetic regulators during the terminal exit from pluripotency.
2022-10-31 | GSE196137 | GEO
Project description:Schizosaccharomyces pombe Clp1 is a Cdc14-family phosphatase that reverses mitotic Cdk1 phosphorylation. Despite evolutionary conservation, Clp1’s mammalian orthologs do not share this function. Rather, higher eukaryotic Cdc14 enzymes act in DNA repair, ciliogenesis, and gene regulation. To examine if Clp1 regulates gene expression, we compared the transcriptional profiles of cells lacking Clp1 function to that of wildtype. Because clp1∆ cells are sensitive to the actin depolymerizing drug, LatrunculinA, we also investigated whether a transcriptional response was involved. Our results indicate that Clp1 does not detectably affect gene expression and highlight the organism-specific functions of this conserved phosphatase family.
2024-03-11 | GSE255124 | GEO
Project description:The Cdc14 phosphatase plays a key role in organising the intricate choreography of mitosis and cell division. In order to understand the role of Cdc14 in the human fungal pathogen Candida albicans we used quantitative proteomics to identify interacting proteins of CaCdc14. We used an orthogonal approach of a substrate trapping mutant combined with affinity purification-mass spectrometry analysis using stable isotope labelling in cell culture (SILAC). The results identified 126 proteins that interact with Cdc14 of which 80% are novel. These provide further insight into the function of Cdc14, highlighting roles in regulating the attachment of the mitotic spindle to kinetochores, mitotic exit, cytokinesis, licensing of DNA replication by re-activating pre-replication complexes, and DNA repair. Five Cdc14-interacting proteins with previously unknown functions localized to the Spindle Pole Bodies (SPBs). Intriguingly, there was suggestive evidence that Cdc14 substrates may include components of the ergosterol biosynthesis pathway targeted by azole anti-fungal drugs Thus we have greatly expanded the set of known substrates of Cdc14 by which it carries out these roles.
2019-11-12 | PXD009581 | Pride
Project description:We have previously shown that the Cdc14 phosphatase is essential for an efficient repair of a DNA lesion, however we still missing how the phosphatase exerts this molecular functions and what are its targets during the repair process. To identify Cdc14 phospho-targets in response to DNA damage, we performed mass spectrometry analysis of Wild-type and Cdc14 deficient cells before and after inducing a single DSBs by expressing the HO endonuclease. Wild-type and a thermosensitive allele cdc14-1 were grown overnight and blocked in G2/M by using nocodazole to avoid cell cycle-dependent changes in protein phosphorylation between both strains. After the block was attained, cells were transfer to 37C to deplete Cdc14 activity prior HO induction. By, using this approach we have screened for proteins containing quantitate low levels of phosphorylated residues after the induction of the DNA lesion that occurs only when Cdc14 is active.
2016-12-22 | PXD004966 | Pride
Project description:Given that Cdc14 enzymes are so highly conserved, we questioned whether budding yeast Cdc14 could really have such a different influence on Cdk site dephosphorylation. We used quantitative phosphoproteomics to directly measure the in vivo specificity of budding yeast Cdc14 and found that it very selectively dephosphorylates a distinct sub-class of Cdk sites and does not catalyze widespread Cdk site dephosphorylation as widely believed.
2017-07-13 | PXD005237 | Pride
Project description:Genomic instability is a common feature found in cancer cells. Accordingly, many tumor suppressor genes identified in familiar cancer syndromes are involved in the maintenance of the stability of the genome during every cell division, and are commonly referred to as caretakers. Inactivating mutations and epigenetic silencing of caretakers are thought to be the most important mechanism that explains cancer-related genome instability. However, little is known of whether transient inactivation of caretaker proteins could trigger genome instability and, if so, what types of instability would occur. In this work, we show that a brief and reversible inactivation, during just one cell cycle, of the key phosphatase Cdc14 in the model organism Saccharomyces cerevisiae is enough to result in diploid cells with multiple gross chromosomal rearrangements and changes in ploidy. Interestingly, we observed that such transient inactivation yields a characteristic fingerprint whereby trisomies are often found in small-sized chromosomes and gross chromosome rearrangements, often associated with concomitant loss of heterozygosity (LOH), are mainly detected on the rDNA-bearing chromosome XII. Taking into account the key role of Cdc14 in preventing anaphase bridges, resetting replication origins and controlling spindle dynamics in a well-defined window within anaphase, we speculate that its transient inactivation causes cells to go through a single mitotic catastrophe with irreversible consequences for the genome stability of the progeny.
2015-05-05 | GSE68530 | GEO