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The p38 Mitogen-activated Protein Kinase Augments Nucleotide Excision Repair by Mediating DDB2 Degradation and Chromatin Relaxation
Published in American Society for Biochemistry & Molecular Biology (ASBMB)
2008
PMID: 18806262
Volume: 283
   
Issue: 47
Pages: 32553 - 32561
Abstract

The p38 MAPK is a family of serine/threonine protein kinases that play important roles in cellular responses to external stress signals, e.g. UV irradiation. To assess the role of p38 MAPK pathway in nucleotide excision repair (NER), the most versatile DNA repair pathway, we determined the efficiency of NER in cells treated with p38 MAPK inhibitor SB203580 and found that p38 MAPK is required for the prompt repair of UV-induced DNA damage CPD. We further investigated the possible mechanism through which p38 MAPK regulates NER and found that p38 MAPK mediates UV-induced histone H3 acetylation and chromatin relaxation. Moreover, p38 MAPK also regulates UV-induced DDB2 ubiquitylation and degradation via phosphorylation of the target protein. Finally, our results showed that p38 MAPK is required for the recruitment of NER factors XPC and TFIIH to UV-induced DNA damage sites. We conclude that p38 MAPK regulates chromatin remodeling as well as DDB2 degradation for facilitating NER factor assembly.

About the journal
JournalData powered by TypesetJournal of Biological Chemistry
PublisherData powered by TypesetAmerican Society for Biochemistry & Molecular Biology (ASBMB)
ISSN0021-9258
Impact Factor6.540
Open AccessNo
Citation StyleVancouver
Sherpa RoMEO Archiving PolicyGreen