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Investigation of the PCNA binding site in the DNA of cells in S-phase

ABSTRACT: In a cell, g-tubulin establishes a cellular network of threads named g-string meshwork. However, the functions of this meshwork remain to be determined. We investigated the traits of the meshwork and show that g-strings have the ability to connect the cytoplasm and the nuclear DNA together. We also show that g-tubulin has a role in determining the positioning of PCNA during DNA-replication.

ORGANISM(S): Homo sapiens

PROVIDER: GSE113094 | GEO | 2021/06/18

REPOSITORIES: GEO

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Investigation of the gamma-tubulin binding site in the nuclear and mitochondrial DNA of cells in S-phase

Project description:In a cell, g-tubulin establishes a cellular network of threads named g-string meshwork. However, the functions of this meshwork remain to be determined. We investigated the traits of the meshwork and show that g-strings have the ability to connect the cytoplasm and the mitochondrial DNA together. We also show that g-tubulin has a role in the maintenance of the mitochondrial meshwork and homeostasis as reduced levels of g-tubulin or impairment of its GTPase domain disrupts the mitochondria network and alters both their respiratory capacity and the expression of mitochondria-related genes. By contrast, reduced mitochondria number or increased protein levels of g-tubulin DNA-binding domain favour the association of g-tubulin with mitochondria. Our results demonstrate that g-tubulin is an important mitochondrial structural component that maintains the mitochondria meshwork, providing mitochondria with a cellular infrastructure. We propose that g-tubulin provides a cytoskeletal element that maintains mitochondria homeostasis and gives form to the mitochondria meshwork. Keywords: Genome binding/occupancy profiling by high throughput sequencing

2018-04-04 | GSE107975 | GEO

The g-tubulin meshwork assists to the transport of cytosolic PCNA to chromatin in mammalian cells

Project description:Changes in the location of g-tubulin ensure cell survival and preserve genome integrity. We investigated whether the nuclear accumulation of g-tubulin facilitates the transport of proliferating cell nuclear antigen (PCNA) between the cytosolic and the nuclear compartment in mammalian cells. We found that the g-tubulin meshwork assists to the recruitment of PCNA to chromatin. Also, decreased levels of g-tubulin reduce the nuclear pool of PCNA. In addition, the g-tubulin C terminus encodes a PCNA-interacting peptide (PIP) motif, and a g-tubulin–PIP-mutant affects the nuclear accumulation of PCNA. In a cell-free system, PCNA and g-tubulin formed a complex. In tumors, there is a significant positive correlation between TUBG1 and PCNA expression. Thus, we report a novel mechanism that constitutes the basis for tumor growth by which the g-tubulin meshwork maintains indefinite proliferation by acting as an opportune scaffold for the transport of PCNA from the cytosol to the chromatin.

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The g-tubulin meshwork assists to the transport of cytosolic PCNA to chromatin in mammalian cells

Project description:Changes in the location of g-tubulin ensure cell survival and preserve genome integrity. We investigated whether the nuclear accumulation of g-tubulin facilitates the transport of proliferating cell nuclear antigen (PCNA) between the cytosolic and the nuclear compartment in mammalian cells. We found that the g-tubulin meshwork assists to the recruitment of PCNA to chromatin. Also, decreased levels of g-tubulin affected the nuclear pool of PCNA. In addition, the g-tubulin C terminus encodes a PCNA-interacting peptide (PIP) motif, and a g-tubulin–PIP-mutant affects the nuclear accumulation of PCNA. In a cell-free system, PCNA and g-tubulin formed a complex. In tumors, there is a significant positive correlation between TUBG1 and PCNA expression. Thus, we report a novel mechanism that constitutes the basis for tumor growth by which the g-tubulin meshwork maintains indefinite proliferation by acting as an opportune scaffold for the transport of PCNA from the cytosol to the chromatin.

2021-06-18 | GSE173732 | GEO

The g-tubulin meshwork assists to the transport of cytosolic PCNA to chromatin in mammalian cells

Project description:The g-tubulin meshwork assists to the transport of cytosolic PCNA to chromatin in mammalian cells

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The g-tubulin meshwork assists to the transport of cytosolic PCNA to chromatin in mammalian cells

Project description:The g-tubulin meshwork assists to the transport of cytosolic PCNA to chromatin in mammalian cells

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Investigation of the gamma-tubulin and PCNA binding site in the DNA of cells in S-phase

Project description:Investigation of the gamma-tubulin and PCNA binding site in the DNA of cells in S-phase

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Investigation of the PCNA binding site in the DNA of cells in S-phase

Project description:Investigation of the PCNA binding site in the DNA of cells in S-phase

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RNA-seq of PCNA WT/PyMT mammary tumor cell and PCNA 211F mammary tumor cell

Project description:To further understand the cellular function of PCNA Y211 phosphrylation, we have profiled RNA expression from our transgenic mouse model derived mammary tumor cell.

2021-08-24 | GSE150513 | GEO

Ubiquitinated PCNA drives USP1 synthetic lethality in cancer

Project description:CRISPR Cas9-based functional genomics screening is a powerful approach for identifying and characterizing novel oncology drug targets. Here, we elucidate the synthetic lethal mechanism of deubiquitinating enzyme USP1 in cancers with underlying DNA damage vulnerabilities, specifically BRCA1/2 mutant tumors and a subset of BRCA1/2 wild-type (WT) tumors. In sensitive cells, pharmacological inhibition of USP1 leads to decreased DNA synthesis concomitant with the induction of S-phase-specific DNA damage. Genome-wide CRISPR-Cas9 screens identified RAD18 and UBE2K, which promote PCNA mono- and polyubiquitination respectively, as downstream mediators of USP1 dependency. The accumulation of mono- and polyubiquitinated PCNA following USP1 inhibition was associated with a reduction in total PCNA protein levels. Ectopic expression of WT and ubiquitin-dead K164R PCNA reversed USP1 inhibitor sensitivity. Our results demonstrate, for the first time, that USP1 dependency hinges on the aberrant processing of mono- and polyubiquitinated PCNA. Moreover, this mechanism of USP1 dependency extends beyond BRCA1/2 mutant tumors to a novel subset of BRCA1/2 WT cancer enriched in ovarian and lung lineages. We further show PARP and USP1 inhibition are strongly synergistic in BRCA1/2 mutant cell lines and xenograft models. We postulate USP1 dependency unveils a previously uncharacterized vulnerability linked to post-translational modifications of PCNA. Taken together, USP1 inhibition may represent a unique therapeutic strategy for BRCA1/2 mutant tumors and a subset of BRCA1/2 WT tumors.

2022-09-27 | GSE214121 | GEO

Differently expressed gene analysis in HeLa cells expressing high levels of phosphorylated PCNA

Project description:Cells expressing phosphorylation-mimicking PCNA, PCNA-Y211D, show elevated hallmarks specific to the epithelial-mesenchymal transition (EMT), including the upregulation of EMT-promoting factor Snail and the downregulation of EMT-inhibitory factors E-cadherin and GSK3β. These cells exhibit active cell migration and also undergo G2/M arrest. Interestingly, all of these EMT-associated activities require the activation of ATM and Akt, as inactivating these protein kinases by gene knockdown or inhibitors blocks EMT-associated signaling and cell migration. We conclude that PCNA phosphorylation promotes cancer progression via the ATM/Akt/GSK3β/Snail signaling pathway. This study, therefore, identifies a novel PCNA function and provides the molecular basis of phosphorylated PCNA-mediated cancer development and progression.

2019-02-28 | GSE127276 | GEO

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