Publications by authors named "Najat Magroun"

Several members of the Poly(ADP-ribose) polymerase (PARP) family are essential regulators of genome integrity, actively prospected as drug targets for cancer therapy. Among them, PARP3 is well characterized for its functions in double-strand break repair and mitotis. Here we report that PARP3 also plays an integral role in TGFβ and reactive oxygen species (ROS) dependent epithelial-to-mesenchymal transition (EMT) and stem-like cell properties in human mammary epithelial and breast cancer cells.

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Poly(ADP-ribose) polymerase 1 (PARP1, also known as ARTD1) is an abundant nuclear enzyme that plays important roles in DNA repair, gene transcription, and differentiation through the modulation of chromatin structure and function. In this work we identify a physical and functional poly(ADP-ribose)-mediated interaction of PARP1 with the E3 ubiquitin ligase UHRF1 (also known as NP95, ICBP90) that influences two UHRF1-regulated cellular processes. On the one hand, we uncovered a cooperative interplay between PARP1 and UHRF1 in the accumulation of the heterochromatin repressive mark H4K20me3.

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Article Synopsis
  • The repair of toxic double-strand breaks (DSB) is essential for preserving genome integrity, with the main repair mechanisms being homologous recombination (HR) and nonhomologous end joining (C-NHEJ and A-EJ).
  • The choice of repair pathway is influenced by DNA end resection, which favors HR and can promote error-prone repair processes like A-EJ when resection is excessive.
  • PARP3 plays a crucial role in regulating DNA repair decisions by interacting with Ku proteins, and its depletion disrupts the balance between DNA repair pathways, leading to increased sensitivity to DSB-inducing anti-cancer treatments.
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Article Synopsis
  • Poly(ADP-ribose) polymerase-1 (Parp-1) and SirT1 are essential enzymes that help maintain genome integrity and regulate chromatin in cells.
  • Disrupting both Parp-1 and SirT1 genes in mice leads to higher post-natal mortality and telomeric abnormalities, indicating their crucial roles during development.
  • The absence of Parp-1 can improve some structural issues in cells lacking SirT1, suggesting these proteins work together in responding to DNA damage and managing specific cellular structures.
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