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Figure 1 | Breast Cancer Research

Figure 1

From: Tyrosine kinase signalling in breast cancer: Epidermal growth factor receptor and c-Src interactions in breast cancer

Figure 1

Structure of c-Src. C-Src is the prototype of a large family of cytoplasmic tyrosine kinases that associate with cellular membranes through lipid modifications at their amino-termini. As a linear molecule, the relationship between the various domains can be seen: an amino-terminal membrane-association domain that contains the site of myristylation; a unique domain that exhibits the widest sequence divergence among family members of any of the domains; an SH3 domain that binds polyproline motifs on target molecules; a SH2 domain that binds phosphotyrosine residues on target molecules; a SH2/kinase linker; the catalytic domain; and the negative regulatory domain that contains the predominant site of tyrosine phosphorylation on the inactive molecule (Y527 in chicken, Y530 in human). Mutations that abrogate myristylation, the SH2 domain, and the catalytic activity were shown to reduce EGF-stimulated DNA synthesis in C3H10T½ murine fibroblasts, providing evidence for the involvement of c-Src in mitogenic pathways [18*].

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