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A human XPC protein interactome--a resource

Abigail Lubin, Ling Zhang, Hua Chen

  • 1Department of Biochemistry and Molecular Biology, University of Miami Miller School of Medicine, Miami, FL 33156, USA. fgong@med.miami.edu.

International Journal of Molecular Sciences
|December 25, 2013
PubMed

Insights

Researchers identified new proteins interacting with Xeroderma pigmentosum complementation group C (XPC), a key DNA repair protein. This discovery sheds light on XPC

Area of Science:

  • Molecular Biology
  • Genetics
  • Biochemistry

Background:

  • Global genome nucleotide excision repair (GG-NER) removes DNA damage from non-transcribed regions.
  • Xeroderma pigmentosum complementation group C (XPC) protein is crucial for GG-NER pathway damage recognition.
  • XPC dysfunction causes xeroderma pigmentosum (XP), a disease linked to sun sensitivity and cancer risk.

Purpose of the Study:

  • To comprehensively characterize the XPC protein interactome.
  • To understand XPC's role in DNA damage recognition within chromatin.
  • To explore XPC's involvement in XP pathogenesis.

Main Methods:

  • High-throughput yeast two-hybrid screening to identify XPC interactors.
  • Co-immunoprecipitation (co-IP) to validate protein interactions.
  • Knockdown experiments in human cells to assess functional impact.

Main Results:

  • Identified 49 novel XPC interactors involved in DNA repair, replication, proteolysis, transcription, and metabolism.
  • Validated the interaction between XPC and OTUD4.
  • Demonstrated that OTUD4 knockdown affects ubiquitinated XPC levels, suggesting a role in XPC recycling.

Conclusions:

  • The XPC interactome provides a valuable resource for further research into XPC function.
  • OTUD4, a deubiquitinase, likely plays a role in regulating XPC levels through ubiquitination.
  • XPC may possess additional, uncharacterized cellular functions beyond its known role in DNA repair.

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