Chicken embryo fibroblasts (CEF) which are transformed by pp60[src] show an increase in the steady-state levels of tyrosine-phosphorylated proteins. One of these proteins is the Actin Filament-Associated Protein, AFAP110. This protein forms a stable complex with activated pp60[src] via the SH3 and SH2 domains of the src protein. However, tyrosine phosphorylation of AFAP requires only the intact src SH3 domain. AFAP is associated with actin stress fibers in normal CE cells, but following transformation by pp60[src], AFAP becomes localized in rosette-like structures known as podosomes. Several sequence motifs within AFAP110 are predicted to bind to SH2 and to SH3 domains. In vitro analysis of AFAP in normal cell extracts demonstrated that it binds less efficiently to Src SH2-containing fusion proteins than does AFAP from src-transformed cell extracts.
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