TY - JOUR
T1 - An SH3 domain-mediated interaction between the phagocyte NADPH oxidase factors p40phox and p47phox
AU - Ito, Takashi
AU - Nakamura, Rika
AU - Sumimoto, Hideki
AU - Takeshige, Koichiro
AU - Sakaki, Yoshiyuki
N1 - Funding Information:
Acknowledgements. We are grateful to N. Aoyama (University of Tokyo) and Y. Kage (Kyushu University) for their excellent technical assistance. We also thank Dr. D. Kang (Kyushu University) for helpful discussion. This work was partly supported by grants from the Ministry of Education, Science, Sports and Culture of Japan, and from Uehera Memorial Foundation.
PY - 1996/5/6
Y1 - 1996/5/6
N2 - The phagocyte NADPH oxidase is activated during phagocytosis to produce superoxide, following assembly of a membrane-integrated cytochrome b558 with cytosolic proteins, p47phox, p67phox and p40phox, each containing Src homology 3 (SH3) domains. While both p47phox and p67phox are indispensable for the oxidase activity, role of p40phox remains obscure. Here we study interaction between p40phox and p47phox by two independent methods, a two-hybrid system in the yeast and an in vitro binding assay using purified proteins. The present results show that the interaction is mediated via binding of the SH3 domain of p40phox to a C-terminal proline-rich region of p47phox. This proline-rich region is also the target for binding of p67phox, and the SH3 domain of p40phox can inhibit the binding of the C-terminal one of p67phox to p47phox.
AB - The phagocyte NADPH oxidase is activated during phagocytosis to produce superoxide, following assembly of a membrane-integrated cytochrome b558 with cytosolic proteins, p47phox, p67phox and p40phox, each containing Src homology 3 (SH3) domains. While both p47phox and p67phox are indispensable for the oxidase activity, role of p40phox remains obscure. Here we study interaction between p40phox and p47phox by two independent methods, a two-hybrid system in the yeast and an in vitro binding assay using purified proteins. The present results show that the interaction is mediated via binding of the SH3 domain of p40phox to a C-terminal proline-rich region of p47phox. This proline-rich region is also the target for binding of p67phox, and the SH3 domain of p40phox can inhibit the binding of the C-terminal one of p67phox to p47phox.
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U2 - 10.1016/0014-5793(96)00387-0
DO - 10.1016/0014-5793(96)00387-0
M3 - Article
C2 - 8647257
AN - SCOPUS:0029931527
SN - 0014-5793
VL - 385
SP - 229
EP - 232
JO - FEBS Letters
JF - FEBS Letters
IS - 3
ER -