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Phosphoregulation of RAD51AP1 function in homology-directed repair.

Neelam Sharma1, Mollie E Uhrig2, Youngho Kwon3

  • 1Department of Environmental and Radiological Health Sciences, Colorado State University, Fort Collins, Colorado, USA.

The Journal of Biological Chemistry
|January 14, 2026
PubMed
Summary
This summary is machine-generated.

Phosphorylation regulates RAD51AP1

Keywords:
CDK1/2DNA bindingRAD51AP1cell cyclehomology-directed repair

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Area of Science:

  • Molecular Biology
  • Genetics
  • Biochemistry

Background:

  • Homology-directed DNA repair (HDR) is crucial for maintaining genome stability and suppressing tumors.
  • RAD51AP1 interacts with RAD51 and is overexpressed in various cancers, correlating with poor prognosis.

Purpose of the Study:

  • To investigate the role of RAD51AP1 phosphorylation in regulating its activity.
  • To elucidate the mechanism by which RAD51AP1 participates in DNA repair.

Main Methods:

  • Site-directed mutagenesis to create RAD51AP1 phosphorylation mutants (S277/282A and S277/282D).
  • Electrophoretic mobility shift assays (EMSAs) to assess DNA binding.
  • In-cell assays to evaluate RAD51AP1 function in DNA repair and toxicity.

Main Results:

  • RAD51AP1 mutants with alanine substitutions at S277/282 (S277/282A) showed enhanced D-loop formation and avid DNA binding.
  • Conversely, phosphomimetic RAD51AP1 mutants (S277/282D) fully rescued RAD51AP1 deficiency in cellular assays.
  • RAD51AP1-S277 was identified as a target of CDK2.

Conclusions:

  • RAD51AP1 activity is regulated by phosphorylation at S277/282.
  • Phosphorylation likely controls RAD51AP1 flexibility, enabling its dynamic role in HDR.
  • CDK2-mediated phosphorylation of RAD51AP1 is a key regulatory mechanism in DNA repair.