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SerpinB2 is involved in cellular response upon UV irradiation
Hajnalka Majoros1, Zsuzsanna Ujfaludi1, Barbara Nikolett Borsos1
1Department of Biochemistry and Molecular Biology, University of Szeged, Faculty of Science and Informatics, Szeged, Hungary.
Scientific Reports
|February 28, 2019
Summary
SerpinB2 (SPB2) protein is upregulated by UV light and moves to DNA damage sites. SPB2 regulates the removal of repair complexes, potentially preventing cancerous malformations in UV-induced DNA repair.
Area of Science:
- Molecular Biology
- Genetics
- Dermatology
Background:
- Ultraviolet (UV) light causes DNA damage, specifically pyrimidine dimers.
- Nucleotide excision repair (NER) removes UV-induced DNA damage, but downstream regulation remains unclear.
- SerpinB2 (SPB2) is identified as a gene upregulated by UV irradiation.
Purpose of the Study:
- To investigate the role of SerpinB2 (SPB2) in the UV-induced DNA damage response.
- To elucidate the regulatory mechanisms of downstream nucleotide excision repair (NER) pathway.
Main Methods:
- High-throughput screening to identify UV-responsive genes.
- Analysis of SPB2 mRNA and protein levels post-UV irradiation.
- Cellular localization studies (cytoplasmic to nuclear translocation, foci formation).
- Co-localization assays with NER proteins (XPB).
- Analysis of SPB2 association with ubiquitylated proteins.
Main Results:
- SPB2 expression (mRNA and protein) significantly increases after UV irradiation in various cell types.
- UV damage induces SPB2 translocation to the nucleus and formation of damage-induced foci.
- SPB2 co-localizes with XPB at UV-induced repair sites.
- UV irradiation enhances SPB2 association with ubiquitylated proteins.
- Altered SPB2 localization is observed in basal cell carcinoma cells.
Conclusions:
- SPB2 plays a novel role in the UV-induced NER pathway.
- SPB2 regulates the dissociation of repair complexes from damaged DNA sites.
- Dysregulation of SPB2 may contribute to cancerous malformations following UV exposure.
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