Epidermal growth factor receptor phosphorylates protein kinase C {delta} at Tyr332 to form a trimeric complex with p66Shc in the H2O2-stimulated cells
| Autor: | Masakatsu Morita, Toshiyoshi Yamamoto, Ushio Kikkawa, Yasuo Fukami, Hidenori Matsuzaki |
|---|---|
| Rok vydání: | 2007 |
| Předmět: |
Src Homology 2 Domain-Containing
Transforming Protein 1 environment and public health Biochemistry Tropomyosin receptor kinase C Receptor tyrosine kinase chemistry.chemical_compound Epidermal growth factor Chlorocebus aethiops Animals Phosphorylation Molecular Biology Protein kinase C Adaptor Proteins Signal Transducing biology Tyrosine phosphorylation General Medicine Hydrogen Peroxide Molecular biology Cell biology Rats ErbB Receptors enzymes and coenzymes (carbohydrates) Protein Kinase C-delta chemistry Shc Signaling Adaptor Proteins ROR1 COS Cells biology.protein Tyrosine biological phenomena cell phenomena and immunity Tyrosine kinase |
| Zdroj: | Journal of biochemistry. 143(1) |
| ISSN: | 0021-924X |
| Popis: | Protein kinase C (PKC) delta is phosphorylated at Tyr311 and Tyr332 and its catalytic activity is enhanced in the H(2)O(2)-stimulated cells, but the enzymes that recognize these tyrosine residues, especially Tyr332, have been remained to be clarified. The analysis of the endogenous proteins in COS-7 cells revealed that PKCdelta binds to p66Shc, an adaptor protein containing two phosphotyrosine-binding domains, in a manner dependent on its tyrosine phosphorylation upon H(2)O(2) stimulation. The studies using the mutated PKCdelta clarified that PKCdelta associates with p66Shc through the phosphorylated Tyr332 residue. Epidermal growth factor (EGF) receptor was detected in the anti-p66Shc immunoprecipitate prepared from the H(2)O(2)-stimulated cells, and this receptor-type tyrosine kinase phosphorylated PKCdelta at Tyr332 in vitro. PKCdelta was, however, not tyrosine phosphorylated in the EGF-stimulated cells, whereas H(2)O(2)-induced tyrosine phosphorylation of PKCdelta and its association with p66Shc were strongly suppressed by EGF receptor kinase inhibitors such as AG1478 and PD153035. These results indicate that EGF receptor phosphorylates PKCdelta at Tyr332 in the H(2)O(2)-stimulated but not in the growth-factor treated cells, and suggest that PKCdelta in the complex with p66Shc and EGF receptor may play a role in the stress-signalling pathway. |
| Databáze: | OpenAIRE |
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