p130Cas/BCAR1 plays a role in cell transformation and cancer progression and alterations of p130Cas/BCAR1 expression and the resulting activation of selective signalling are determinants for the occurrence of different types of human tumors.

[11] p130Cas/BCAR1 is a member of the Cas family (Crk-associated substrate) of adaptor proteins which is characterized by the presence of multiple conserved motifs for protein–protein interactions, and by extensive tyrosine and serine phosphorylations.

[14][15] p130Cas/BCAR1 can undergo extensive changes in tyrosine phosphorylation that occur predominantly in the 15 YxxP repeats within the substrate domain and represent the major post-translational modification of p130Cas/BCAR1.

p130Cas/BCAR1 tyrosine phosphorylation can result from a diverse range of extracellular stimuli, including growth factors, integrin activation, vasoactive hormones and peptides ligands for G-protein coupled receptors.

[15] Given the ability of p130Cas/BCAR1 scaffold protein to convey and integrate different type of signals and subsequently to regulate key cellular functions such as adhesion, migration, invasion, proliferation and survival, the existence of a strong correlation between deregulated p130Cas/BCAR1 expression and cancer was inferred.

[16] The presence of aberrant levels of hyperphosphorylated p130Cas/BCAR1 strongly promotes cell proliferation, migration, invasion, survival, angiogenesis and drug resistance.

[13] It has been demonstrated that high levels of p130Cas/BCAR1 expression in breast cancer correlate with worse prognosis, increased probability to develop metastasis and resistance to therapy.