The three models could be distinguished on the basis of tyrosine phosphorylation signatures and signalling networks. The functional role of mesenchymal–epithelial transition factor (Met) in a subset of p53-null tumours was interrogated using a selective tyrosine kinase inhibitor (TKI), small interfering RNA (siRNA)–mediated knockdown and cell proliferation assays. Molecular mechanisms underpinning differences in tyrosine phosphorylation were characterised by Western blot analysis and array comparative genomic hybridisation. Pathways and protein–protein interaction networks were identified by bioinformatics analysis.

We applied an immunoaffinity/mass spectrometry workflow to three mouse models: murine stem cell virus-Neu, expressing truncated Neu, the rat orthologue of human epidermal growth factor receptor 2, Her2 (HER2) mouse mammary tumour virus-polyoma virus middle T antigen (PyMT) and the p53 −/− transplant model (p53). This may identify conserved oncogenic pathways and potential therapeutic targets. Although aberrant tyrosine kinase signalling characterises particular breast cancer subtypes, a global analysis of tyrosine phosphorylation in mouse models of breast cancer has not been undertaken to date.

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