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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/RAfOFWXVo3a_vZGFgokRPX70xqBYhp3VP7h3EgtnG0CBc#_4 http://resource.belframework.org/belframework/1.0/knowledge/large_corpus.bel http://purl.org/pav/version 1.4 http://www.tkuhn.ch/bel2nanopub/RAfOFWXVo3a_vZGFgokRPX70xqBYhp3VP7h3EgtnG0CBc#_3 http://www.w3.org/ns/prov#value In searching for a possible linkage between HA-CD44-mediated IQGAP1 signaling and ERK and ER{alpha} function, we demonstrated that IQGAP1-linked ERK2 isolated from SK-OV-3.ipl cells treated with HA was capable of phosphorylating ER{alpha} in vitro (Fig. 5A, bar b). EGF stimulation of MAPKs such as ERK1 and ERK2 has been shown to phosphorylate ER{alpha} at Ser118 in the N-terminal domain and to enhance transcriptional activity. ER{alpha} phosphorylation in vivo (as detected by anti-phospho-ER{alpha} antibody (Ser118)) was also greatly enhanced in SK-OV-3.ipl cells treated with HA.The level of ERE gene activity was low in untreated cells (bar a) or in cells pretreated with anti-CD44 antibody, followed by HA treatment (bar c). 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