Analysis of the interaction between the epidermal growth factor receptor and actin

TL;DRAbstract

It has been shown that the epidermal growth factor receptor (EGFR) can directly interact with F-actin via an actin-binding domain (ABD) located at amino acid residues 984–996. In this study, we investigate the interaction of the EGFR with actin using an actin cosedimentation assay in a reconstituted cell free system. We find that soluble components of the cytosol from A431 cells dramatically enhance the EGFR/actin interaction. This result is found for EGFR purified by EGFR1 immunoprecipitation, over an EGFR1 affinity column or over a wheat germ agglutinin column. This EGFR/actin interaction is shown to be both cytosol protein concentration and actin concentration dependent. Several lines of evidence suggest that this interaction is not mediated by the previously defined ABD of the EGFR but rather requires both the kinase domain and a portion of the C-terminal regulatory domain of the EGFR. Our results suggest the binding of EGFR to F-actin is under the regulation of one or multiple sol

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