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All rights reserved. http://resource.belframework.org/belframework/1.0/knowledge/large_corpus.bel http://purl.org/dc/elements/1.1/title BEL Framework Large Corpus Document http://resource.belframework.org/belframework/1.0/knowledge/large_corpus.bel http://purl.org/pav/authoredBy http://www.tkuhn.ch/bel2nanopub/RAAB6z2Dc1eqT_cKbiBENTPHlfREum1mbHiOaMz7UQLQM#_5 http://resource.belframework.org/belframework/1.0/knowledge/large_corpus.bel http://purl.org/pav/version 1.4 http://www.tkuhn.ch/bel2nanopub/RAAB6z2Dc1eqT_cKbiBENTPHlfREum1mbHiOaMz7UQLQM#_4 http://www.w3.org/ns/prov#value Expression of phase II detoxifying genes is regulated by NF-E2-related factor 2 (Nrf2)-mediated antioxidant response element (ARE) activation. We showed previously that phosphatidylinositol 3 (PI3)-kinase plays an essential role in ARE-mediated rGSTA2 induction by oxidative stress. In view of the fact that the signaling pathway of PI3-kinase controls microfilaments and translocation of actin-associated proteins, the current study was designed to investigate the PI3-kinase-mediated nuclear translocation of Nrf2 and the interaction of Nrf2 with actin. tert-Butylhydroquinone (t-BHQ) caused Nrf2 to translocate into the nucleus in H4IIE cells, which was prevented by pretreatment of the cells with PI3-kinase inhibitors (wortmannin/LY294002). t-BHQ relocalized Nrf2 in concert with changes in actin microfilament architecture, as visualized by superposition of immunochemically stained Nrf2 and fluorescent phalloidin-stained actin. Furthermore, t-BHQ increased the level of nuclear actin, coimmunoprecipitated with Nrf2, which returned to that of control by pretreatment of the cells with PI3-kinase inhibitors. Cytochalasin B, an actin disruptor, alone stimulated actin-mediated nuclear translocation of Nrf2 and induced rGSTA2. In contrast, phalloidin, an agent that prevents actin filaments from depolymerization, inhibited Nrf2 translocation and rGSTA2 induction by t-BHQ. Subcellular fractionation and immunoblot analyses allowed us to detect both 57- and 100-kDa Nrf2. Immunoblot and immunoprecipitation assays showed that the 100-kDa protein comprised both Nrf2 and actin. The present study demonstrates that the PI3-kinase signaling pathway regulates rearrangement of actin microfilaments in response to oxidative stress and that depolymerization of actin causes a complex of Nrf2 bound with actin to translocate into nucleus. http://www.tkuhn.ch/bel2nanopub/RAAB6z2Dc1eqT_cKbiBENTPHlfREum1mbHiOaMz7UQLQM#_4 http://www.w3.org/ns/prov#wasQuotedFrom http://www.ncbi.nlm.nih.gov/pubmed/12391262 http://www.tkuhn.ch/bel2nanopub/RAAB6z2Dc1eqT_cKbiBENTPHlfREum1mbHiOaMz7UQLQM#_5 http://www.w3.org/2000/01/rdf-schema#label Selventa http://www.tkuhn.ch/bel2nanopub/RAAB6z2Dc1eqT_cKbiBENTPHlfREum1mbHiOaMz7UQLQM#assertion http://www.w3.org/ns/prov#hadPrimarySource http://www.ncbi.nlm.nih.gov/pubmed/12391262 http://www.tkuhn.ch/bel2nanopub/RAAB6z2Dc1eqT_cKbiBENTPHlfREum1mbHiOaMz7UQLQM#assertion http://www.w3.org/ns/prov#wasDerivedFrom http://resource.belframework.org/belframework/1.0/knowledge/large_corpus.bel http://www.tkuhn.ch/bel2nanopub/RAAB6z2Dc1eqT_cKbiBENTPHlfREum1mbHiOaMz7UQLQM#assertion http://www.w3.org/ns/prov#wasDerivedFrom http://www.tkuhn.ch/bel2nanopub/RAAB6z2Dc1eqT_cKbiBENTPHlfREum1mbHiOaMz7UQLQM#_4 http://www.tkuhn.ch/bel2nanopub/RAAB6z2Dc1eqT_cKbiBENTPHlfREum1mbHiOaMz7UQLQM#pubinfo http://www.tkuhn.ch/bel2nanopub/RAAB6z2Dc1eqT_cKbiBENTPHlfREum1mbHiOaMz7UQLQM http://purl.org/dc/terms/created 2014-07-03T14:30:06.599+02:00 http://www.tkuhn.ch/bel2nanopub/RAAB6z2Dc1eqT_cKbiBENTPHlfREum1mbHiOaMz7UQLQM http://purl.org/pav/createdBy http://orcid.org/0000-0001-6818-334X http://www.tkuhn.ch/bel2nanopub/RAAB6z2Dc1eqT_cKbiBENTPHlfREum1mbHiOaMz7UQLQM http://purl.org/pav/createdBy http://orcid.org/0000-0002-1267-0234