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RPAP3 interacts with Reptin to regulate UV-induced phosphorylation of H2AX and DNA damage. | LitMetric

RPAP3 interacts with Reptin to regulate UV-induced phosphorylation of H2AX and DNA damage.

J Cell Biochem

Department of Pharmacology, Graduate School of Dentistry, Osaka University, Suita, Osaka, Japan.

Published: April 2009

AI Article Synopsis

Article Abstract

We have previously reported that Monad, a novel WD40 repeat protein, potentiates apoptosis induced by tumor necrosis factor-alpha 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.

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Source
http://dx.doi.org/10.1002/jcb.22073DOI Listing

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