EAST, a novel EGF receptor substrate, associates with focal adhesions and actin fibers.

EAST is a novel epidermal growth factor receptor (EGFR) substrate. It interacts with Eps15, another EGFR substrate which is involved in receptor endocytosis. In this study we show that EAST associates with focal adhesions and actin filaments. First, in immunofluorescence and electron microscopy analysis, an extensive codistribution of EAST with vinculin, paxillin and actin filaments was seen. Second, overexpression of the NH2 terminus of EAST led to a formation of actin-rich microspikes and membrane protrusions. Third, in cosedimentation assay EAST showed a direct association with actin. These results suggest that EAST is involved in the EGFR-regulated reorganization of the actin cytoskeleton and may be part of a link between cytoskeleton and endocytic machinery.