2009年4月
RPAP3 Interacts With Reptin to Regulate UV-Induced Phosphorylation of H2AX and DNA Damage
JOURNAL OF CELLULAR BIOCHEMISTRY
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- 巻
- 106
- 号
- 5
- 開始ページ
- 920
- 終了ページ
- 928
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1002/jcb.22073
- 出版者・発行元
- WILEY
We have previously reported that Monad, a novel WD40 repeat protein, potentiates apoptosis induced by tumor necrosis factor-a and cycloheximide. By affinity purification and mass spectrometry, RNA polymerase II-associated protein 3 (RPAP3) was identified as a Monad binding protein and may function with Monad as a novel modulator of apoptosis pathways. Here we report that Reptin, a highly conserved AAA + ATPase that is part of various chromatin-remodeling complexes, is also involved in the association of RPAP3 by immunoprecipitation and confocal microscopic analysis. Overexpression of RPAP3 induced HEK293 cells to death after UV-irradiation. Loss of RPAP3 by RNAi improved HeLa cell survival after UV-induced DNA damage and attenuated the phosphorylation of H2AX. Depletion of Reptin reduced cell survival and facilitated the phosphorylation on H2AX. These results suggest that RPAP3 modulates UV-induced DNA damage by regulating H2AX phosphorylation. J. Cell. Biochem. 106: 920-928, 2009. (C) 2009 Wiley-Liss, Inc.
- リンク情報
- ID情報
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- DOI : 10.1002/jcb.22073
- ISSN : 0730-2312
- eISSN : 1097-4644
- PubMed ID : 19180575
- Web of Science ID : WOS:000264664800020