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DNA-damage dependent isoform switching modulates RIF1 DNA repair complex assembly and phase separation.

Adenine Si-Hui Koo1, Weiyan Jia1, Sang Hwa Kim1

  • 1Department of Human Oncology, School of Medicine and Public Health, University of Wisconsin-Madison, 1111 Highland Ave, Madison, WI 53705, USA.

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Summary
This summary is machine-generated.

Alternative splicing of RIF1 (RAP1 interacting factor) generates distinct variants that impact DNA repair and genome organization. Exon 32 inclusion is regulated by cell cycle, DNA damage, and specific splicing factors, influencing RIF1 function.

Keywords:
DNA damageRNA binding proteinalternative splicingcell signalingchromatin

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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Genetics

Background:

  • RIF1 (RAP1 interacting factor) is crucial for DNA repair, replication, and nuclear organization.
  • RIF1 exists as two splice variants, RIF1-Long (RIF1-L) and RIF1-Short (RIF1-S), due to alternative splicing of Exon 32 (Ex32).
  • Ex32 encodes a peptide in the RIF1 C-terminal domain, potentially modulating protein function.

Purpose of the Study:

  • To investigate the regulation of Ex32 alternative splicing in RIF1.
  • To characterize the functional differences between RIF1-L and RIF1-S isoforms.
  • To understand how alternative splicing impacts RIF1's role in genome protection.

Main Methods:

  • Analysis of Ex32 inclusion levels under various conditions (DNA damage, cell cycle).
  • Identification of splicing factors regulating Ex32 splicing (e.g., SRSF1, PTBP1, SRSF3).
  • Isoform-specific proteomics and biochemical assays to compare RIF1-L and RIF1-S.

Main Results:

  • Ex32 inclusion is repressed by DNA damage and oncogenesis, peaking during G2/M phase.
  • Splicing factors SRSF1, PTBP1, and SRSF3 directly regulate Ex32 splice-in.
  • RIF1-L shows enhanced association with MDC1 and strengthens its recruitment to DNA damage sites.
  • RIF1 isoforms display distinct phase separation and chromatin-binding properties modulated by CDK1 phosphorylation.

Conclusions:

  • Regulated alternative splicing of RIF1 Exon 32 fine-tunes RIF1 function in response to cellular cues.
  • RIF1-L and RIF1-S isoforms possess distinct properties influencing DNA repair and genome organization.
  • Alternative splicing is a key mechanism controlling RIF1's multifaceted roles in maintaining genome integrity.