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Related Concept Videos

Nuclear Export01:42

Nuclear Export

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The nucleus restricts several proteins within and allows others to pass. The restricted proteins possess a nuclear retention sequence or NRS, anchoring them to the nuclear lamins and preventing their transport to the cytosol. The non-restricted proteins, after their synthesis, are transported to their site of action, such as the cytosol or other organelles, with the help of nuclear export signals or NES.
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In response to DNA damage, cells can pause the cell cycle to assess and repair the breaks. However, the cell must check the DNA at certain critical stages during the cell cycle. If the cell cycle pauses before DNA replication, the cells will contain twice the amount of DNA. On the other hand, if cells arrest after DNA replication but before mitosis, they will contain four times the normal amount of DNA. With a host of specialized proteins at their disposal,cells must use the right protein at...
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In response to DNA damage, cells can pause the cell cycle to assess and repair the breaks. However, the cell must check the DNA at certain critical stages during the cell cycle. If the cell cycle pauses before DNA replication, the cells will contain twice the amount of DNA. On the other hand, if cells arrest after DNA replication but before mitosis, they will contain four times the normal amount of DNA. With a host of specialized proteins at their disposal,cells must use the right protein at...
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Before mRNAs are exported to the cytoplasm, it is crucial to check each mRNA for structural and functional integrity. Eukaryotic cells use several different mechanisms, collectively known as mRNA surveillance, to look for irregularities in mRNAs. Irregular or aberrant mRNA are rapidly degraded by various enzymes. If a defective mRNA escapes the surveillance, it would be translated into a protein which would either be non-functional or not function properly. One of the primary irregularities in...
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DNA Distortion and Damage
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Visualization of DNA Repair Proteins Interaction by Immunofluorescence
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ATM induces MacroD2 nuclear export upon DNA damage.

Barbara Golia1, Giuliana Katharina Moeller1, Gytis Jankevicius1

  • 1Department of Physiological Chemistry, Biomedical Center, Ludwig-Maximilians-Universität München, Planegg-Martinsried 82152, Germany.

Nucleic Acids Research
|January 11, 2017
PubMed
Summary
This summary is machine-generated.

MacroD2, a DNA repair enzyme, is exported from the nucleus after DNA damage, controlled by ATM activity. This regulates ADP-ribosylation, a key DNA repair process, revealing a novel feedback loop.

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Area of Science:

  • Molecular Biology
  • Biochemistry
  • Cell Biology

Background:

  • ADP-ribosylation is a crucial post-translational modification regulating DNA repair.
  • Its levels depend on transferases and hydrolases, but regulation of these enzymes is poorly understood.
  • PARP1/ARDT1 is the only known transferase with regulatory insights.

Purpose of the Study:

  • To investigate the regulation of ADP-ribosylation hydrolases in DNA repair.
  • To elucidate the role of MacroD2 in DNA damage response.
  • To uncover novel interactions between ATM signaling and ADP-ribosylation.

Main Methods:

  • Investigated MacroD2 localization and export upon DNA damage.
  • Utilized ATM activity assays and phosphorylation site analysis.
  • Assessed the impact of MacroD2 nuclear export on DNA lesion recruitment.

Main Results:

  • MacroD2, a mono-ADP-ribosylhydrolase, is exported from the nucleus following DNA damage.
  • This export is induced by ATM (Ataxia-Telangiectasia Mutated) activity.
  • Export depends on ATM-mediated phosphorylation of MacroD2's SQ/TQ motifs.
  • Nuclear export of MacroD2 limits its access to DNA lesions, reducing hydrolase activity at damage sites.

Conclusions:

  • Identified a novel feedback mechanism linking ATM signaling and ADP-ribosylation.
  • MacroD2 nuclear export represents a new regulatory layer in DNA damage response.
  • This finding highlights a direct interplay between ATM activation and ADP-ribosylation dynamics.