@article{4f43c224d21e4bb38a0d66b78151ceb7,
title = "EGF receptor signaling stimulates SRC kinase phosphorylation of clathrin, influencing clathrin redistribution and EGF uptake",
abstract = "Epidermal growth factor (EGF) binding to its receptor causes rapid phosphorylation of the clathrin heavy chain at tyrosine 1477, which lies in a domain controlling clathrin assembly. EGF-mediated clathrin phosphorylation is followed by clathrin redistribution to the cell periphery and is the product of downstream activation of SRC kinase by EGF receptor (EGFR) signaling. In cells lacking SRC kinase, or cells treated with a specific SRC family kinase inhibitor, EGF stimulation of clathrin phosphorylation and redistribution does not occur, and EGF endocytosis is delayed. These observations demonstrate a role for SRC kinase in modification and recruitment of clathrin during ligand-induced EGFR endocytosis and thereby define a novel effector mechanism for regulation of endocytosis by receptor signaling.",
author = "Andrew Wilde and Beattie, {Eric C.} and Lawrence Lem and Riethof, {David A.} and Liu, {Shu Hui} and Mobley, {William C.} and Philippe Soriano and Brodsky, {Frances M.}",
note = "Funding Information: We are grateful to D. O. Morgan for purified recombinant pp60 c-src , G. N. Gill for transfectants expressing wild-type and mutant EGFR and the plasmid encoding the recombinant fusion protein CT-GST, D. Shalloway for the 3T3 transfectant overexpressing pp60 c-src , and T. Nagase for the human CHC cDNA. We also thank A. Sorkin, J. M. Bishop, and J. Brugge for providing antibodies and A. Sorkin, C. Lowell, F. Luton, and D. Slowiejko for helpful discussion. This work was supported by National Institutes of Health grants GM38093 and GM57657 to F. M. B. and a postdoctoral fellowship from the American Heart Association, California affiliate to A. W. We thank M. Von Zastrow and the Carnegie Institution of Washington and Y. Zheng for facilitating completion of this work.",
year = "1999",
month = mar,
day = "5",
doi = "10.1016/S0092-8674(00)80578-4",
language = "English",
volume = "96",
pages = "677--687",
journal = "Cell",
issn = "0092-8674",
publisher = "Elsevier B.V.",
number = "5",
}