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p38-Mediated phosphorylation of Eps15 endocytic adaptor protein |
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| Authors: | Yue Zhou Tomohiro Tanaka Naoyuki Sugiyama Satoru Yokoyama Yuki Kawasaki Tsutomu Sakuma Yasushi Ishihama Ikuo Saiki Hiroaki Sakurai |
| Institution: | 1. Department of Cancer Cell Biology, Graduate School of Medicine and Pharmaceutical Sciences, University of Toyama, Toyama 930-0194, Japan;2. Department of Molecular & Cellular BioAnalysis, Graduate School of Pharmaceutical Sciences, Kyoto University, Sakyo-ku, Kyoto 606-8501, Japan;3. Division of Pathogenic Biochemistry, Institute of Natural Medicine, University of Toyama, Toyama 930-0194, Japan |
| 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: | CME clathrin-mediated endocytosis EGFR epidermal growth factor receptor Eps15 EGFR pathway substrate 15 TAK1 transforming growth factor-β-activated kinase 1 TAB1 TAK1-binding protein 1 TNF-α tumor necrosis factor-α UIM ubiquitin-interacting motif |
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