Key role of EGFR, ErbB2 and PR proteins in gene and protein interactions with Vimentin, FOXC1/2, FAK, and the BRCA1 in prevention of triple negative breast cancer

Studies on protein–protein interactions and RNA–protein interactions between transcription factors and receptors that act as tumor suppressor proteins play key roles in designing new anticancer drugs for treatment. The BRCA1 RING domain exhibits protein–protein interactions with Vimentin, FOXC2, Focal adhesion kinase and EGFR, whereas the EGFR nucleic acid contig shows gene–protein interactions with Vimentin, FOXC2, Focal adhesion kinase and BRCA1. ErbB2 and the progesterone receptor play key roles in protein–protein interactions with the BRCA1 RING domain and ErB2 in TNBC, and the PR nucleic acid contig shows gene–protein interactions with vimentin, FOXC2, focal adhesion kinase and the BRCA1 RING domain, clearly indicating that the transaction of proteins occurs mostly although noncovalent interactions.