EGF Receptor Signaling Stimulates SRC Kinase Phosphorylation of Clathrin, Influencing Clathrin Redistribution and EGF Uptake
| Autor: | David A. Riethof, Shu-Hui Liu, Frances M. Brodsky, Andrew Wilde, Eric C. Beattie, William C. Mobley, Philippe Soriano, Lawrence Lem |
|---|---|
| Rok vydání: | 1999 |
| Předmět: |
Recombinant Fusion Proteins
Molecular Sequence Data Proto-Oncogene Proteins pp60(c-src) Biology Ligands Endocytosis Clathrin General Biochemistry Genetics and Molecular Biology Mice 03 medical and health sciences 0302 clinical medicine Epidermal growth factor Tumor Cells Cultured Animals Humans Amino Acid Sequence Src family kinase Phosphorylation Receptor 030304 developmental biology 0303 health sciences Epidermal Growth Factor Biochemistry Genetics and Molecular Biology(all) Insulin-like growth factor 2 receptor Biological Transport Cell biology ErbB Receptors src-Family Kinases biology.protein Cattle Protein Processing Post-Translational 030217 neurology & neurosurgery Proto-oncogene tyrosine-protein kinase Src |
| Zdroj: | Cell. 96:677-687 |
| ISSN: | 0092-8674 |
| DOI: | 10.1016/s0092-8674(00)80578-4 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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