The network diagram is shown in Figure 1. We constructed connections between various signalling proteins in our basic apoptosis network using the existing literature. HER2 is a cell transmembrane receptor which plays a significant role in breast cancer by suppression of tumour growth. It provides growth signals in PI3KAKT and Ras-MAPK pathways. HER2 also suppresses p53-mediated apoptosis by upregulation of MDM2 by activation of AKT. p53 also participates in promoting apoptosis by sensing DNA damage and can upregulate pro-apoptotic Bcl-2 proteins (e.g. PUMA) as well as suppress IAPs (e.g. survivin) [6]. PUMA is a pro-apoptotic protein and plays crucial roles in apoptosis. Tumour suppressor gene p53 regulates the expression of PUMA. Once activated, PUMA frees the apoptosis regulator Bax and Bak owing to its high affinity with Bcl-2 oncogenic group of proteins. The freed proteins further transduce the apoptotic signals to the mitochondria. This causes the Caspases to be activated and the activated caspases eventually lead to the cell death [7]. Activation of pro-apoptotic BAX/Bak facilitates heme protein cytochrome c being released from the inner mitochondria membrane [8,9]. The cytochrome c further stimulates Casp9, which then stimulates Casp3 and Casp7, which eventually lead to apoptotic cell death [10]. Up-regulation of DAPK induces apoptosis by enhancing response of tumour suppressor p53 whereas down-regulation of DAPK reduces the response of p53 to several oncogenes including c-Myc and E2F-1. The activated form of DAPK further activates the Beclin-1 by phosphorylation. Beclin-1 activation is crucial for Autophagy and also for its crosstalk with apoptosis.