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Journal of Biochemistry Advance Access published online on October 23, 2007
Journal of Biochemistry, doi:10.1093/jb/mvm190
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© 2007 The Japanese Biochemical Society

Epidermal growth factor receptor phosphorylates protein kinase C {delta} at Tyr332 to form a trimeric complex with p66Shc in the H2O2-stimulated cells

Masakatsu Morita1, Hidenori Matsuzaki1, Toshiyoshi Yamamoto1, Yasuo Fukami2 and Ushio Kikkawa1,*

1 Biosignal Research Center, Kobe University, Kobe 657-8501, Japan; and 2 Research Center for Environmental Genomics, Kobe University, Kobe 657-8501, Japan

*To whom correspondence should be addressed: Ushio Kikkawa Biosignal Research Center, Kobe University, 1-1 Rokkodai-cho, Nada-ku, Kobe 657-8501, Japan. Tel: + 81-78-803-5964, Fax: +81-78-803-5972, E-mail: ukikkawa{at}kobe-u.ac.jp

Received August 31, 2007; Accepted September 30, 2007


  Abstract

Protein kinase C (PKC) {delta} is phosphorylated at Tyr311 and Tyr332 and its catalytic activity is enhanced in the H2O2-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 PKC{delta} binds to p66Shc, an adaptor protein containing two phosphotyrosine-binding domains, in a manner dependent on its tyrosine phosphorylation upon H2O2 stimulation. The studies using the mutated PKC{delta} clarified that PKC{delta} associates with p66Shc through the phosphorylated Tyr332 residue. Epidermal growth factor (EGF) receptor was detected in the anti-p66Shc immunoprecipitate prepared from in the H2O2-stimulated cells, and this receptor-type tyrosine kinase phosphorylated PKC{delta} at Tyr332 in vitro. PKC{delta} was, however, not tyrosine phosphorylated in the EGF-stimulated cells, whereas H2O2-induced tyrosine phosphorylation of PKC{delta} 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 PKC{delta} at Tyr332 in the H2O2-stimulated but not in the growth-factor treated cells, and suggest that PKC{delta} in the complex with p66Shc and EGF receptor may play a role in the stress-signaling pathway.

Key Words: complex formation, EGF receptor, hydrogen peroxide, PKC{delta}, Shc


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