@article{ab51ac2622954416bdbd11181d1be1ac,
title = "P38-Mediated phosphorylation of Eps15 endocytic adaptor protein",
abstract = "Epidermal growth factor receptor pathway substrate 15 (Eps15) has been suggested to be involved in the endocytosis of cell surface receptors, including epidermal growth factor receptor (EGFR). Eps15 is phosphorylated at Tyr-849 upon stimulation with EGF during endocytic processes. In the present study, we found that stimulation of HeLa cells with EGF or TNF-α induced transient phosphorylation of Eps15 at Ser-796. Inhibition of p38 completely blocked phosphorylation and recombinant p38α directly phosphorylated the residue. These results demonstrate a novel stress kinase-mediated signaling pathway to Eps15 endocytic adapter protein.",
keywords = "EGF, Eps15, TAK1, TNF-α, p38",
author = "Yue Zhou and Tomohiro Tanaka and Naoyuki Sugiyama and Satoru Yokoyama and Yuki Kawasaki and Tsutomu Sakuma and Yasushi Ishihama and Ikuo Saiki and Hiroaki Sakurai",
note = "Funding Information: We are grateful to Drs. Alexandre Benmerah (INSERM U1016, Institut Cochin, Paris, France) and Pier Paolo Di Fiore (IFOM, Fondazione Istituto FIRC di Oncologia Molecolare, Milan, Italy) for providing GFP-Eps15 expression plasmids and triple knocked-down HeLa cells, respectively. This work was supported in part by Grants-in-Aid for Scientific Research on Innovative Areas and Scientific Research (C) from the Ministry of Education, Culture, Sports, Science and Technology, Japan , and a Grant-in-Aid for the Cooperative Research Project from the Institute of Natural Medicine , University of Toyama in 2011. ",
year = "2014",
month = jan,
day = "3",
doi = "10.1016/j.febslet.2013.11.020",
language = "英語",
volume = "588",
pages = "131--137",
journal = "FEBS Letters",
issn = "0014-5793",
publisher = "John Wiley and Sons Inc.",
number = "1",
}