Proteomics

Dataset Information

0

Comparative phosphoproteomic analysis of HeLa cells in response to etoposide or to a combination of etoposide and the ATR inhibitor VE821


ABSTRACT: To investigate the regulation of protein phosphorylation during the DNA damage response and the role of ATR kinase activity, we performed a comparative phosphoproteomic analysis of HeLa cells treated with etoposide alone or in combination with the ATR inhibitor VE821. Etoposide is a topoisomerase II inhibitor that induces DNA double-strand breaks, activating the DNA damage signaling cascade. We focused particularly on phosphorylation events associated with Treacle (TCOF1), a nucleolar protein implicated in the regulation of rDNA transcription and nucleolar DNA damage response. Quantitative mass spectrometry-based phosphoproteomics was used to identify and quantify global phosphorylation changes under both treatment conditions. This dataset enables the identification of ATR-dependent phosphorylation sites and may provide insights into the molecular mechanisms underlying nucleolar stress responses and the coordination of DNA repair processes.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Malignant Cell, Cell Culture

DISEASE(S): Cervical Cancer

SUBMITTER: Georgij Arapidi  

LAB HEAD: Georgij Arapidi

PROVIDER: PXD067042 | Pride | 2026-05-25

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
Omar_20211228_SH366-Sh367_Phosphoproteome-ATR-inhibitor_Experiment_Condensed.sf3 Other
Sh-366-1.dat Other
Sh-366-1.mgf Mgf
Sh-366-1.mzid Mzid
Sh-366-1.mzid_Sh-366-1.MGF Mzid
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Publications


Ribosomal DNA (rDNA) arrays are among the most highly transcribed repetitive regions of the genome and therefore require specialized mechanisms to maintain their stability. The nucleolar DNA damage response (n-DDR) safeguards rDNA integrity and is coordinated by the repair scaffold TOPBP1 and the fibrillar center (FC) protein Treacle. Here, we show that Treacle promotes phase separation of TOPBP1 within the FC to establish a spatially confined signaling platform that amplifies nucleolar DDR sign  ...[more]

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