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Related Concept Videos

DNA Damage can Stall the Cell Cycle02:36

DNA Damage can Stall the Cell Cycle

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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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DNA Damage Can Stall the Cell Cycle02:36

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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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DNA replication is initiated at sites containing predefined DNA sequences known as origins of replication. DNA is unwound at these sites by the minichromosome maintenance (MCM) helicase and other factors such as Cdc45 and the associated GINS complex.The unwound single strands are protected by replication protein A (RPA) until DNA polymerase starts synthesizing DNA at the 5’ end of the strand in the same direction as the replication fork. To prevent the replication fork from falling apart,...
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Translesion DNA Polymerases02:10

Translesion DNA Polymerases

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Translesion (TLS) polymerases rescue stalled DNA polymerases at sites of damaged bases by replacing the replicative polymerase and installing a nucleotide across the damaged site. Doing so, TLS allows additional time for the cell to repair the damage before resuming regular DNA replication.
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Homologous Recombination02:31

Homologous Recombination

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The basic reaction of homologous recombination (HR) involves two chromatids that contain DNA sequences sharing a significant stretch of identity. One of these sequences uses a strand from another as a template to synthesize DNA in an enzyme-catalyzed reaction. The final product is a novel amalgamation of the two substrates. To ensure an accurate recombination of sequences, HR is restricted to the S and G2 phases of the cell cycle. At these stages, the DNA has been replicated already and the...
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Since the discovery of the two BER pathways, there has been a debate about how a cell chooses one pathway over the other and the factors determining this selection. Numerous in vitro experiments have pointed out multiple determinants for the sub-pathway selection. These are:
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Updated: Jan 13, 2026

Visualization of DNA Repair Proteins Interaction by Immunofluorescence
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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, Madison, Wisconsin, USA.

The Journal of Biological Chemistry
|January 6, 2026
PubMed
Summary
This summary is machine-generated.

RAP1 interacting factor 1 (RIF1) alternative splicing generates distinct RIF1 isoforms (RIF1-L and RIF1-S) that diversify its roles in DNA repair and genome protection. DNA damage promotes RIF1-S, impacting protein function.

Keywords:
DNA damageMDC1RIF1RNA binding proteinalternative splicingcell signalingchromatin

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Area of Science:

  • Molecular Biology
  • Genetics
  • Cell Biology

Background:

  • The protein RAP1 interacting factor 1 (RIF1) plays crucial roles in DNA double-strand break repair, DNA replication, and nuclear organization.
  • The precise mechanisms by which RIF1 executes its diverse functions remain incompletely understood.

Purpose of the Study:

  • To investigate how alternative splicing of RIF1 contributes to its functional diversification.
  • To elucidate the role of RIF1 isoforms in response to DNA damage and their implications in cancer.

Main Methods:

  • Analysis of alternative splicing events in RIF1, focusing on a cassette exon (Ex32) in the C-terminal domain (CTD).
  • Identification of splicing factors (SRSF1, SRSF3, SRSF7) regulating RIF1 alternative splicing.
  • Isoform-specific proteomic analyses to identify binding partners and functional differences between RIF1-L and RIF1-S.
  • Investigation of RIF1 CTD phase separation activity and chromatin retention dynamics.

Main Results:

  • Alternative splicing of RIF1 Ex32 generates RIF1-Long (RIF1-L) and RIF1-Short (RIF1-S) isoforms with distinct functional characteristics.
  • DNA damage inhibits Ex32 splice-in, increasing RIF1-S expression, a phenomenon observed in primary cancers.
  • RIF1-L preferentially associates with mediator of DNA damage checkpoint 1 (MDC1) and enhances MDC1 focus formation.
  • The Ser/Lys-rich cassette in RIF1-L stabilizes CTD phase separation activity and enhances chromatin retention, modulated by CDK1 phosphorylation.

Conclusions:

  • DNA damage-dependent alternative splicing of RIF1 is a key mechanism for functional diversification.
  • RIF1 isoforms play distinct roles in genome protection, with RIF1-L contributing to DNA damage response and RIF1-S potentially linked to cancer progression.
  • These findings provide novel insights into RIF1 regulation and its multifaceted roles in maintaining genome integrity.