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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/RAefrl9op8HNiX2oaZbXSFh-64dHZqU3QFfvwf77v8ZwU#_7 http://resource.belframework.org/belframework/1.0/knowledge/large_corpus.bel http://purl.org/pav/version 1.4 http://www.tkuhn.ch/bel2nanopub/RAefrl9op8HNiX2oaZbXSFh-64dHZqU3QFfvwf77v8ZwU#_6 http://www.w3.org/ns/prov#value More recently, ERBB transactivation has been shown to involve other physiological ligands (FIG. 2). The binding of WNT to its seven-pass membrane receptor Frizzled (FZD) transactivates EGFR. The mechanism seems to be similar to that described for GPCRs, as it is rapid and blocked by metalloproteinase inhibitors; however, the target ligand has not been identified. WNT?FZD-mediated transactivation has been observed in normal mammary cells43 and in breast cancer cells (T. Schlange and N.E.H., unpublished observations). Oestradiol (E2) bindingto plasma-membrane-associated oestrogen receptor (ER) has also been shown to rapidly transactivate ERBBs. According to one report, E2-stimulated activation of MMP2 and MMP9 leads to the release of HB-EGF. 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