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EAST, a novel EGF receptor substrate, associates with focal adhesions and actin fibers
Author(s) -
Lohi Olli,
Lehto Veli-Pekka
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)01171-5
Subject(s) - vinculin , focal adhesion , cytoskeleton , microbiology and biotechnology , actin , endocytic cycle , actin cytoskeleton , endocytosis , epidermal growth factor receptor , paxillin , cytoplasm , chemistry , biology , receptor , cell , signal transduction , biochemistry
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 NH 2 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.