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RNA-binding protein RBM14 regulates dissociation and association of non-homologous end joining proteins

Nicholas E Simon1, Ming Yuan1,2, Mihoko Kai1

  • 1a Department of Radiation Oncology, Department of Pathology , Johns Hopkins University, School of Medicine , Baltimore , MD , USA.

Cell Cycle (Georgetown, Tex.)
|April 21, 2017
PubMed

Insights

RNA-binding protein RBM14 is crucial for DNA repair by facilitating the recruitment of key proteins to damaged sites. This ensures efficient double-strand break repair, preventing disease-associated DNA damage accumulation.

Area of Science:

  • Molecular Biology
  • Genetics
  • Cell Biology

Background:

  • Defects in the DNA damage response (DDR) are linked to diseases like cancer and neurodegenerative disorders.
  • RNA-binding proteins (RBPs) are increasingly implicated in DDR, but their specific roles are not fully understood.
  • Previous work identified RNA-binding protein RBM14's requirement for non-homologous end joining (NHEJ).

Purpose of the Study:

  • To elucidate the function of RNA-binding protein RBM14 in the DNA damage response pathway.
  • To investigate RBM14's role in the non-homologous end joining (NHEJ) process upon DNA damage.

Main Methods:

  • Chromatin immunoprecipitation assays to assess protein recruitment and release.
  • Analysis of double-strand break accumulation in cells with altered RBM14 function.
  • Investigating the interaction of RBM14 with NHEJ factors like XRCC4, XLF, and KU proteins.

Main Results:

  • RBM14 is essential for the efficient recruitment of XRCC4 and XLF to chromatin following DNA damage.
  • RBM14 mediates the release of KU proteins from chromatin after DNA damage.
  • Impaired RBM14 function leads to the accumulation of unrepaired double-strand breaks (DSBs).

Conclusions:

  • RBM14 plays a critical regulatory role in the non-homologous end joining (NHEJ) pathway of DNA repair.
  • RBM14's function in protein dynamics at DNA damage sites is vital for maintaining genomic stability.
  • Understanding RBM14's role in DDR opens new avenues for therapeutic strategies targeting diseases with DNA repair deficiencies.
Keywords:
DSB repairNHEJRNA-binding protein

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