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All rights reserved. http://resource.belframework.org/belframework/20131211/knowledge/large_corpus.bel http://purl.org/dc/elements/1.1/title BEL Framework Large Corpus Document http://resource.belframework.org/belframework/20131211/knowledge/large_corpus.bel http://purl.org/pav/authoredBy http://www.tkuhn.ch/bel2nanopub/RA3d6BQNhjMkeCl655I9CvO7h9vFf8oRqN-A1e-Rbxbu8#_8 http://resource.belframework.org/belframework/20131211/knowledge/large_corpus.bel http://purl.org/pav/version 20131211 http://www.tkuhn.ch/bel2nanopub/RA3d6BQNhjMkeCl655I9CvO7h9vFf8oRqN-A1e-Rbxbu8#_7 http://www.w3.org/ns/prov#value To investigate how MET activates ERBB3 tyrosine phosphorylation, we first expressed ERBB3 alone or in combination with MET in Chinese hamster ovary (CHO) cells, which normally do not express detectable levels of EGFR, ERBB2, or ERBB3. Coexpression of MET and ERBB3 resulted in marked phosphorylation of ERBB3 (Fig. 3D). This phosphorylation could be blocked with PHA-665752 but not with high concentrations of gefitinib (3 mM), lapatinib (3 mM) or the SRC family kinase inhibitor PP2 (10 mM). In addition, phosphorylated ERBB3 coimmunoprecipitated with p85 in a MET kinase–dependent manner (fig. 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